Ephrin A3: Difference between revisions

EFNA3
Identifiers
Aliases	EFNA3, EFL2, EPLG3, Ehk1-L, LERK3, ephrin A3
External IDs	OMIM: 601381; MGI: 106644; HomoloGene: 3635; GeneCards: EFNA3; OMA:EFNA3 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	155,087,538 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	89,322,965 bp
RNA expression pattern
	Top expressed in
	skin of leg; ; skin of abdomen; ; skin of arm; ; hair follicle; ; Region I of hippocampus proper; ; cervix epithelium; ; orbitofrontal cortex; ; prefrontal cortex; ; parotid gland; ; nucleus accumbens;
	Top expressed in
	lip; ; perirhinal cortex; ; entorhinal cortex; ; chorion; ; nasal epithelium; ; olfactory epithelium; ; subiculum; ; skin of external ear; ; dentate gyrus of hippocampal formation granule cell; ; esophagus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transmembrane-ephrin receptor activity; protein binding; ephrin receptor binding;
Cellular component	anchored component of membrane; plasma membrane; integral component of plasma membrane; membrane; intrinsic component of plasma membrane;
Biological process	cell-cell signaling; ephrin receptor signaling pathway; axon guidance; negative regulation of angiogenesis; regulation of neuron differentiation; positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	1944
	13638
	ENSG00000143590
	ENSMUSG00000028039
	P52797
	O08545
	NM_004952
	NM_010108
	NP_004943
NP_034238; NP_001364045; NP_001364046; NP_001364047; NP_001364048;
	NP_001364049; NP_001364050
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 14:43, 11 October 2022

Ephrin A3 is a protein that in humans is encoded by the EFNA3 gene.^[5]^[6]

This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143590 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028039 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW (Jan 1997). "The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3". Genomics. 33 (2): 277–82. doi:10.1006/geno.1996.0192. PMID 8660976.
^ ^a ^b "Entrez Gene: EFNA3 ephrin-A3".

Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development". Annu. Rev. Neurosci. 21: 309–45. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499.
Zhou R (1998). "The Eph family receptors and ligands". Pharmacol. Ther. 77 (3): 151–81. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626.
Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis". Development. 126 (10): 2033–44. doi:10.1242/dev.126.10.2033. PMID 10207129.
Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly". Int. Rev. Cytol. International Review of Cytology. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN 978-0-12-364600-2. PMID 10730216.
Xu Q, Mellitzer G, Wilkinson DG (2001). "Roles of Eph receptors and ephrins in segmental patterning". Philos. Trans. R. Soc. Lond. B Biol. Sci. 355 (1399): 993–1002. doi:10.1098/rstb.2000.0635. PMC 1692797. PMID 11128993.
Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. doi:10.1038/35058515. PMID 11256076. S2CID 205014301.
Kozlosky CJ, Maraskovsky E, McGrew JT, et al. (1995). "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins". Oncogene. 10 (2): 299–306. PMID 7838529.{{cite journal}}: CS1 maint: numeric names: authors list (link)
Davis S, Gale NW, Aldrich TH, et al. (1994). "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science. 266 (5186): 816–9. Bibcode:1994Sci...266..816D. doi:10.1126/science.7973638. PMID 7973638.
Gale NW, Holland SJ, Valenzuela DM, et al. (1996). "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron. 17 (1): 9–19. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474. S2CID 1075856.
Ephnomenclaturecommittee (1997). "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell. 90 (3): 403–4. doi:10.1016/S0092-8674(00)80500-0. PMID 9267020. S2CID 26773768.
Janis LS, Cassidy RM, Kromer LF (1999). "Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum". J. Neurosci. 19 (12): 4962–71. doi:10.1523/JNEUROSCI.19-12-04962.1999. PMC 6782661. PMID 10366629.
Stein E, Savaskan NE, Ninnemann O, et al. (1999). "A role for the Eph ligand ephrin-A3 in entorhino-hippocampal axon targeting". J. Neurosci. 19 (20): 8885–93. doi:10.1523/JNEUROSCI.19-20-08885.1999. PMC 6782767. PMID 10516308.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143590 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028039 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8660976-5] Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW (Jan 1997). "The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3". Genomics. 33 (2): 277–82. doi:10.1006/geno.1996.0192. PMID 8660976.

[entrez-6] "Entrez Gene: EFNA3 ephrin-A3".

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
+{{Short description|Protein-coding gene in the species Homo sapiens}}
-{{PBB|geneid=1944}}
+{{Infobox_gene}}
-'''Ephrin-A3''' is a [[protein]] that in humans is encoded by the ''EFNA3'' [[gene]].<ref name="pmid8660976">{{cite journal | author = Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW | title = The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3 | journal = Genomics | volume = 33 | issue = 2 | pages = 277–82 |date=Jan 1997 | pmid = 8660976 | pmc =  | doi = 10.1006/geno.1996.0192 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EFNA3 ephrin-A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1944| accessdate = }}</ref>
+'''Ephrin A3''' is a [[protein]] that in humans is encoded by the ''EFNA3'' [[gene]].<ref name="pmid8660976">{{cite journal | vauthors = Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW | title = The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3 | journal = Genomics | volume = 33 | issue = 2 | pages = 277–82 |date=Jan 1997 | pmid = 8660976 | doi = 10.1006/geno.1996.0192 | url = https://zenodo.org/record/1229677 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EFNA3 ephrin-A3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1944}}</ref>
+This gene encodes a member of the [[ephrin]] (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine [[kinase]]s and have been implicated in mediating developmental events, especially in the [[nervous system]] and in [[erythropoiesis]].  Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane [[protein]]s. This gene encodes an EFNA class ephrin.<ref name="entrez" />
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB Summary
-| section_title =
-| summary_text = This gene encodes a member of the [[ephrin]] (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine [[kinase]]s and have been implicated in mediating developmental events, especially in the nervous system and in [[erythropoiesis]].  Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane [[protein]]s. This gene encodes an EFNA class ephrin.<ref name="entrez" />
-}}
 ==References==
 {{reflist}}
 ==Further reading==
 {{refbegin | 2}}
+*{{cite journal  | vauthors=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development |journal=Annu. Rev. Neurosci. |volume=21 |pages= 309–45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
-{{PBB_Further_reading
-| citations =
-*{{cite journal  | author=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development |journal=Annu. Rev. Neurosci. |volume=21 |issue=  |pages= 309–45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
 *{{cite journal  | author=Zhou R |title=The Eph family receptors and ligands |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151–81 |year= 1998 |pmid= 9576626 |doi=10.1016/S0163-7258(97)00112-5  }}
-*{{cite journal  | author=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |pmid= 10207129 |doi=  }}
+*{{cite journal  | vauthors=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |doi=10.1242/dev.126.10.2033 |pmid= 10207129 }}
-*{{cite journal  | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly |journal=Int. Rev. Cytol. |volume=196 |issue=  |pages= 177–244 |year= 2000 |pmid= 10730216 |doi=10.1016/S0074-7696(00)96005-4  | series=International Review of Cytology  | isbn=978-0-12-364600-2  }}
+*{{cite journal  | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly |journal=Int. Rev. Cytol. |volume=196 |pages= 177–244 |year= 2000 |pmid= 10730216 |doi=10.1016/S0074-7696(00)96005-4  | series=International Review of Cytology  | isbn=978-0-12-364600-2  }}
-*{{cite journal  | author=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635  | pmc=1692797 }}
+*{{cite journal  | vauthors=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning |journal=Philos. Trans. R. Soc. Lond. B Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635  | pmc=1692797 }}
-*{{cite journal  | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=10.1038/35058515  }}
+*{{cite journal  | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=10.1038/35058515  |s2cid=205014301 }}
-*{{cite journal  | author=Kozlosky CJ |title=Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins |journal=Oncogene |volume=10 |issue= 2 |pages= 299–306 |year= 1995 |pmid= 7838529 |doi=  |name-list-format=vanc| author2=Maraskovsky E  | author3=McGrew JT  | display-authors=3  | last4=Vandenbos  | first4=T  | last5=Teepe  | first5=M  | last6=Lyman  | first6=SD  | last7=Srinivasan  | first7=S  | last8=Fletcher  | first8=FA  | last9=Gayle Rb  | first9=3rd  }}
+*{{cite journal  | author=Kozlosky CJ |title=Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins |journal=Oncogene |volume=10 |issue= 2 |pages= 299–306 |year= 1995 |pmid= 7838529 |name-list-style=vanc| author2=Maraskovsky E  | author3=McGrew JT  | display-authors=3  | last4=Vandenbos  | first4=T  | last5=Teepe  | first5=M  | last6=Lyman  | first6=SD  | last7=Srinivasan  | first7=S  | last8=Fletcher  | first8=FA  | last9=Gayle Rb  | first9=3rd  }}
-*{{cite journal  | author=Davis S |title=Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity |journal=Science |volume=266 |issue= 5186 |pages= 816–9 |year= 1994 |pmid= 7973638 |doi=10.1126/science.7973638  |name-list-format=vanc| author2=Gale NW  | author3=Aldrich TH  | display-authors=3  | last4=Maisonpierre  | first4=P.  | last5=Lhotak  | first5=V  | last6=Pawson  | first6=T  | last7=Goldfarb  | first7=M  | last8=Yancopoulos  | first8=G.  }}
+*{{cite journal  | author=Davis S |title=Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity |journal=Science |volume=266 |issue= 5186 |pages= 816–9 |year= 1994 |pmid= 7973638 |doi=10.1126/science.7973638  |name-list-style=vanc| author2=Gale NW  | author3=Aldrich TH  | display-authors=3  | last4=Maisonpierre  | first4=P.  | last5=Lhotak  | first5=V  | last6=Pawson  | first6=T  | last7=Goldfarb  | first7=M  | last8=Yancopoulos  | first8=G.  |bibcode=1994Sci...266..816D }}
-*{{cite journal  | author=Gale NW |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=10.1016/S0896-6273(00)80276-7  |name-list-format=vanc| author2=Holland SJ  | author3=Valenzuela DM  | display-authors=3  | last4=Flenniken  | first4=Ann  | last5=Pan  | first5=Li  | last6=Ryan  | first6=Terrence E  | last7=Henkemeyer  | first7=Mark  | last8=Strebhardt  | first8=Klaus  | last9=Hirai  | first9=Hisamaru  }}
+*{{cite journal  | author=Gale NW |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=10.1016/S0896-6273(00)80276-7  |name-list-style=vanc| author2=Holland SJ  | author3=Valenzuela DM  | display-authors=3  | last4=Flenniken  | first4=Ann  | last5=Pan  | first5=Li  | last6=Ryan  | first6=Terrence E  | last7=Henkemeyer  | first7=Mark  | last8=Strebhardt  | first8=Klaus  | last9=Hirai  | first9=Hisamaru  |s2cid=1075856 | doi-access=free  }}
-*{{cite journal  | author= Ephnomenclaturecommittee,|title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=10.1016/S0092-8674(00)80500-0  }}
+*{{cite journal  | author= Ephnomenclaturecommittee|title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=10.1016/S0092-8674(00)80500-0  |s2cid=26773768 |doi-access=free }}
-*{{cite journal  | author=Janis LS, Cassidy RM, Kromer LF |title=Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum |journal=J. Neurosci. |volume=19 |issue= 12 |pages= 4962–71 |year= 1999 |pmid= 10366629 |doi=  }}
+*{{cite journal  | vauthors=Janis LS, Cassidy RM, Kromer LF |title=Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum |journal=J. Neurosci. |volume=19 |issue= 12 |pages= 4962–71 |year= 1999 |pmid= 10366629 |doi=  10.1523/JNEUROSCI.19-12-04962.1999|pmc=6782661 |doi-access=free }}
-*{{cite journal  | author=Stein E |title=A role for the Eph ligand ephrin-A3 in entorhino-hippocampal axon targeting |journal=J. Neurosci. |volume=19 |issue= 20 |pages= 8885–93 |year= 1999 |pmid= 10516308 |doi=  |name-list-format=vanc| author2=Savaskan NE  | author3=Ninnemann O  | display-authors=3  | last4=Nitsch  | first4=R  | last5=Zhou  | first5=R  | last6=Skutella  | first6=T  }}
+*{{cite journal  | author=Stein E |title=A role for the Eph ligand ephrin-A3 in entorhino-hippocampal axon targeting |journal=J. Neurosci. |volume=19 |issue= 20 |pages= 8885–93 |year= 1999 |pmid= 10516308 |doi=  10.1523/JNEUROSCI.19-20-08885.1999|name-list-style=vanc| author2=Savaskan NE  | author3=Ninnemann O  | display-authors=3  | last4=Nitsch  | first4=R  | last5=Zhou  | first5=R  | last6=Skutella  | first6=T  |pmc=6782767 | doi-access=free}}
-*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
+*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-style=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD |bibcode=2002PNAS...9916899M |doi-access=free }}
-}}
 {{refend}}
-{{gene-1-stub}}
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
-{{PBB Controls
-| update_page = yes
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 {{Intercellular signaling peptides and proteins}}
+{{Growth factor receptor modulators}}
+{{gene-1-stub}}

v t e Intercellular signaling peptides and proteins / ligands
Growth factors	Epidermal growth factor Fibroblast growth factor Nerve growth factor Platelet-derived growth factor Transforming growth factor beta superfamily Vascular endothelial growth factor
Ephrin	EFNA1 EFNA2 EFNA3 EFNA4 EFNA5 EFNB1 EFNB2 EFNB3
Other	Adipokine Agouti signaling protein Agouti-related protein Angiogenic protein CCN intercellular signaling protein Cysteine-rich protein 61 Connective tissue growth factor Nephroblastoma overexpressed protein Cytokine Endothelin EDN1 EDN2 EDN3 Hedgehog protein Interferon Kinin Parathyroid hormone-related protein Semaphorin Somatomedin Tolloid-like metalloproteinase Tumor necrosis factor Wnt protein
see also extracellular ligand disorders