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Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (AD56) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)

 ADA15_MOUSE             Reviewed;         864 AA.
O88839; A4ZYV2; Q3TDN7; Q3U7C2; Q3UE21; Q8C7Z0; Q91VS9; Q9QYL2;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
14-NOV-2003, sequence version 2.
12-SEP-2018, entry version 188.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 15;
Short=ADAM 15;
EC=3.4.24.-;
AltName: Full=AD56;
AltName: Full=Metalloprotease RGD disintegrin protein;
AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15;
Short=MDC-15;
AltName: Full=Metargidin;
Flags: Precursor;
Name=Adam15; Synonyms=Mdc15;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND PROTEOLYTIC PROCESSING.
TISSUE=Lung;
PubMed=9748307; DOI=10.1074/jbc.273.40.26236;
Lum L., Reid M.S., Blobel C.P.;
"Intracellular maturation of the mouse metalloprotease disintegrin
MDC15.";
J. Biol. Chem. 273:26236-26247(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Myeloid, and Myeloma;
PubMed=13679040; DOI=10.1016/j.bbrc.2003.08.070;
Shimizu E., Yasui A., Matsuura K., Hijiya N., Higuchi Y., Yamamoto S.;
"Structure and expression of the murine ADAM 15 gene and its splice
variants, and difference of interaction between their cytoplasmic
domains and Src family proteins.";
Biochem. Biophys. Res. Commun. 309:779-785(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow macrophage, Cerebellum, and Dendritic cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 207-694 (ISOFORMS 1/2/3), FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=18390692; DOI=10.1530/REP-07-0300;
Pasten-Hidalgo K., Hernandez-Rivas R., Roa-Espitia A.L.,
Sanchez-Gutierrez M., Martinez-Perez F., Monrroy A.O.,
Hernandez-Gonzalez E.O., Mujica A.;
"Presence, processing, and localization of mouse ADAM15 during sperm
maturation and the role of its disintegrin domain during sperm-egg
binding.";
Reproduction 136:41-51(2008).
[6]
INTERACTION WITH ENDOPHILIN I AND SNX9.
PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
two SH3 domain-containing proteins, endophilin I and SH3PX1.";
J. Biol. Chem. 274:31693-31699(1999).
[7]
FUNCTION, INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND ALPHA9-BETA1, AND
MUTAGENESIS OF ARG-482; ASP-489; LEU-490; PRO-491; GLU-492 AND
PHE-493.
PubMed=11882657; DOI=10.1074/jbc.M200086200;
Eto K., Huet C., Tarui T., Kupriyanov S., Liu H.Z.,
Puzon-McLaughlin W., Zhang X.P., Sheppard D., Engvall E., Takada Y.;
"Functional classification of ADAMs based on a conserved motif for
binding to integrin alpha 9beta 1: implications for sperm-egg binding
and other cell interactions.";
J. Biol. Chem. 277:17804-17810(2002).
[8]
FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=12897135; DOI=10.1128/MCB.23.16.5614-5624.2003;
Horiuchi K., Weskamp G., Lum L., Hammes H.P., Cai H., Brodie T.A.,
Ludwig T., Chiusaroli R., Baron R., Preissner K.T., Manova K.,
Blobel C.P.;
"Potential role for ADAM15 in pathological neovascularization in
mice.";
Mol. Cell. Biol. 23:5614-5624(2003).
[9]
FUNCTION.
PubMed=15818704; DOI=10.1002/art.20974;
Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., Burkhardt H.;
"Homeostatic effects of the metalloproteinase disintegrin ADAM15 in
degenerative cartilage remodeling.";
Arthritis Rheum. 52:1100-1109(2005).
[10]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=18381816; DOI=10.1096/fj.07-099283;
Xie B., Shen J., Dong A., Swaim M., Hackett S.F., Wyder L.,
Worpenberg S., Barbieri S., Campochiaro P.A.;
"An Adam15 amplification loop promotes vascular endothelial growth
factor-induced ocular neovascularization.";
FASEB J. 22:2775-2783(2008).
-!- FUNCTION: Active metalloproteinase with gelatinolytic and
collagenolytic activity. Plays a role in the wound healing
process. Mediates both heterotypic intraepithelial cell/T-cell
interactions and homotypic T-cell aggregation. Inhibits beta-1
integrin-mediated cell adhesion and migration of airway smooth
muscle cells. Suppresses cell motility on or towards fibronectin
possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell
surface expression via ERK1/2 inactivation. Cleaves E-cadherin in
response to growth factor deprivation. Plays a role in glomerular
cell migration (By similarity). Plays a role in pathological
neovascularization. May play a role in cartilage remodeling. May
be proteolytically processed, during sperm epididymal maturation
and the acrosome reaction. May play a role in sperm-egg binding
through its disintegrin domain. Interactions with egg membrane
could be mediated via binding between the disintegrin-like domain
to one or more integrin receptors on the egg. {ECO:0000250,
ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135,
ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- SUBUNIT: Interacts specifically with Src family protein-tyrosine
kinases (PTKs) (By similarity). Interacts with ITAGV-ITGB3
(vitronectin receptor). Interacts with SH3GL2 and SNX9; this
interaction occurs preferentially with ADAM15 precursor, rather
than the processed form, suggesting it occurs in a secretory
pathway compartment prior to the medial Golgi. Interacts with
ITAG9-ITGB1. Interacts with SH3PXD2A (By similarity). Interacts
with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN,
MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endomembrane system
{ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18390692}. Cell junction, adherens junction
{ECO:0000250}. Cell projection, cilium, flagellum
{ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory
vesicle, acrosome {ECO:0000269|PubMed:18390692}. Note=The majority
of the protein is localized in a perinuclear compartment which may
correspond to the trans-Golgi network or the late endosome. The
pro-protein is the major detectable form on the cell surface,
whereas the majority of the protein in the cell is processed.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=ADAM15v2;
IsoId=O88839-1; Sequence=Displayed;
Name=2; Synonyms=ADAM15v1;
IsoId=O88839-2; Sequence=VSP_008880;
Name=3; Synonyms=ADAM15;
IsoId=O88839-3; Sequence=VSP_008881;
Name=4;
IsoId=O88839-4; Sequence=VSP_008879;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed moderately in pericytes of retina.
Expressed in testis and in spermatozoa from the caput, corpus, and
cauda epididymis, as well as in non-capacitated and acrosome-
reacted sperm (at protein level). Highly expressed in heart,
brain, lung, and kidney. Expressed at lower levels in spleen,
liver, testis and muscle. {ECO:0000269|PubMed:18381816,
ECO:0000269|PubMed:18390692}.
-!- DEVELOPMENTAL STAGE: At E13.5, strongly expressed in the
developing vasculature of the endocardium. At P17, expressed
throughout the retina (at protein level). At E9.5 and thereafter,
prominently expressed in the vasculature, including in ventral and
dorsal aorta and the caudal artery. In developing heart, detected
in endocardium and blood vessels of the ventricle, bulbus
arteriosus, and atrium. Also highly expressed in hypertrophic
cells of the developing bone. In adult, expressed prominently in
brain, including in hippocampus, cerebellum, pons, thalamus,
cortex, and olfactory bulb. {ECO:0000269|PubMed:12897135,
ECO:0000269|PubMed:18381816}.
-!- INDUCTION: By hypoxic stimulus in retina (at protein level). Up-
regulated by VEGF in retina. {ECO:0000269|PubMed:12897135,
ECO:0000269|PubMed:18381816}.
-!- DOMAIN: The cytoplasmic domain is required for SH3GL2- and SNX9-
binding.
-!- DOMAIN: Disintegrin domain binds to integrin alphaV-beta3.
{ECO:0000250}.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase. An
additional membrane proximal site of cleavage affects a small
percentage of the proteins and results in disulfide-linked
fragments. The prodomain is apparently cleaved in several
positions that are N-terminal of the furin cleavage site.
{ECO:0000269|PubMed:9748307}.
-!- PTM: May be partially sialylated.
-!- PTM: Phosphorylation increases association with PTKs.
{ECO:0000250}.
-!- MISCELLANEOUS: Mice targeted for deletion of the first 27 amino
acids of the ADAM15 N-terminal sequence are viable and fertile,
showing no major developmental defects and displaying normal
mortality or morbidity. These mutant mice, however, exhibit
significantly reduced ischemia-induced retinal neovascularization,
choroidal neovascularization at rupture sites in Bruch's membrane,
and VEGF-induced subretinal neovascularization, and develop
significantly smaller tumors following implantation of B16F0
melanoma cells. Aging mutant mice exhibit accelerated development
of osteoarthritic lesions in knee joints.
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EMBL; AF006196; AAC61896.1; -; mRNA.
EMBL; AB022089; BAA88903.1; -; Genomic_DNA.
EMBL; AK048901; BAC33485.1; -; mRNA.
EMBL; AK149796; BAE29090.1; -; mRNA.
EMBL; AK151804; BAE30703.1; -; mRNA.
EMBL; AK152725; BAE31447.1; -; mRNA.
EMBL; AK170101; BAE41564.1; -; mRNA.
EMBL; BC009132; AAH09132.1; -; mRNA.
EMBL; EF506571; ABP73662.1; -; mRNA.
CCDS; CCDS17502.1; -. [O88839-1]
CCDS; CCDS17503.1; -. [O88839-3]
RefSeq; NP_001032811.2; NM_001037722.3. [O88839-1]
RefSeq; NP_033744.1; NM_009614.3. [O88839-3]
RefSeq; XP_006500981.1; XM_006500918.1. [O88839-2]
UniGene; Mm.274049; -.
UniGene; Mm.470104; -.
ProteinModelPortal; O88839; -.
SMR; O88839; -.
IntAct; O88839; 3.
MINT; O88839; -.
STRING; 10090.ENSMUSP00000029676; -.
MEROPS; M12.215; -.
iPTMnet; O88839; -.
PhosphoSitePlus; O88839; -.
SwissPalm; O88839; -.
MaxQB; O88839; -.
PaxDb; O88839; -.
PeptideAtlas; O88839; -.
PRIDE; O88839; -.
Ensembl; ENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041. [O88839-1]
Ensembl; ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041. [O88839-3]
Ensembl; ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041. [O88839-4]
Ensembl; ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041. [O88839-2]
Ensembl; ENSMUST00000184651; ENSMUSP00000139147; ENSMUSG00000028041. [O88839-1]
GeneID; 11490; -.
KEGG; mmu:11490; -.
UCSC; uc008pyv.1; mouse. [O88839-1]
UCSC; uc008pyw.1; mouse. [O88839-3]
CTD; 8751; -.
MGI; MGI:1333882; Adam15.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00910000144014; -.
HOVERGEN; HBG006978; -.
InParanoid; O88839; -.
KO; K06836; -.
OMA; HGVCDSN; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; O88839; -.
TreeFam; TF314733; -.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-8941237; Invadopodia formation.
PRO; PR:O88839; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028041; Expressed in 240 organ(s), highest expression level in bone marrow macrophage.
Genevisible; O88839; MM.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; ISO:MGI.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0002418; P:immune response to tumor cell; ISO:MGI.
GO; GO:0045087; P:innate immune response; ISO:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
GO; GO:1900121; P:negative regulation of receptor binding; ISO:MGI.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR033605; ADAM15.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
PANTHER; PTHR11905:SF130; PTHR11905:SF130; 1.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Cell adhesion; Cell junction;
Cell projection; Cilium; Cleavage on pair of basic residues;
Collagen degradation; Complete proteome; Cytoplasmic vesicle;
Disulfide bond; EGF-like domain; Flagellum; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
Reference proteome; SH3-binding; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 207 {ECO:0000305}.
/FTId=PRO_0000029084.
CHAIN 208 864 Disintegrin and metalloproteinase domain-
containing protein 15.
/FTId=PRO_0000029085.
TOPO_DOM 208 696 Extracellular. {ECO:0000255}.
TRANSMEM 697 717 Helical. {ECO:0000255}.
TOPO_DOM 718 864 Cytoplasmic. {ECO:0000255}.
DOMAIN 214 415 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 422 509 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 658 686 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 177 184 Cysteine switch. {ECO:0000250}.
MOTIF 816 822 SH3-binding. {ECO:0000255}.
MOTIF 851 857 SH3-binding. {ECO:0000255}.
COMPBIAS 510 657 Cys-rich.
COMPBIAS 699 712 Poly-Leu.
ACT_SITE 350 350 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 179 179 Zinc; in inhibited form. {ECO:0000250}.
METAL 349 349 Zinc; catalytic. {ECO:0000255}.
METAL 353 353 Zinc; catalytic. {ECO:0000255}.
METAL 359 359 Zinc; catalytic. {ECO:0000255}.
SITE 289 290 Cleavage; by furin. {ECO:0000255}.
MOD_RES 716 716 Phosphotyrosine; by HCK and LCK.
{ECO:0000250|UniProtKB:Q13444}.
MOD_RES 736 736 Phosphotyrosine; by HCK and LCK.
{ECO:0000250|UniProtKB:Q13444}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 393 393 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 607 607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 612 612 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 324 410 {ECO:0000250}.
DISULFID 366 394 {ECO:0000250}.
DISULFID 368 377 {ECO:0000250}.
DISULFID 481 501 {ECO:0000250}.
DISULFID 658 668 {ECO:0000250}.
DISULFID 662 674 {ECO:0000250}.
DISULFID 676 685 {ECO:0000250}.
VAR_SEQ 415 830 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008879.
VAR_SEQ 761 809 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9748307}.
/FTId=VSP_008881.
VAR_SEQ 761 785 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_008880.
MUTAGEN 482 482 R->A: Reduced binding to CHO cells
expressing ITAG9-ITGB1.
{ECO:0000269|PubMed:11882657}.
MUTAGEN 489 489 D->A: Reduced binding to CHO cells
expressing ITAG9-ITGB1.
{ECO:0000269|PubMed:11882657}.
MUTAGEN 490 490 L->A: Reduced binding to CHO cells
expressing ITAG9-ITGB1.
{ECO:0000269|PubMed:11882657}.
MUTAGEN 491 491 P->A: Reduced binding to CHO cells
expressing ITAG9-ITGB1.
{ECO:0000269|PubMed:11882657}.
MUTAGEN 492 492 E->A: Reduced binding to CHO cells
expressing ITAG9-ITGB1.
{ECO:0000269|PubMed:11882657}.
MUTAGEN 493 493 F->A: Reduced binding to CHO cells
expressing ITAG9-ITGB1.
{ECO:0000269|PubMed:11882657}.
CONFLICT 21 22 PP -> RR (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 51 51 Q -> H (in Ref. 3; BAE29090).
{ECO:0000305}.
CONFLICT 73 73 S -> P (in Ref. 3; BAE41564).
{ECO:0000305}.
CONFLICT 443 443 E -> Q (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 459 459 G -> E (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 564 565 SP -> T (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 654 654 G -> E (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 660 660 R -> S (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 703 703 L -> R (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 712 712 L -> R (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 729 729 L -> R (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 830 830 Q -> R (in Ref. 3; BAE41564).
{ECO:0000305}.
CONFLICT 846 846 L -> S (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 852 854 PAP -> AAS (in Ref. 2; BAA88903).
{ECO:0000305}.
CONFLICT 859 859 A -> P (in Ref. 2; BAA88903).
{ECO:0000305}.
SEQUENCE 864 AA; 92664 MW; B1CBEB923463BB15 CRC64;
MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV QDSPPMSLAD
VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW YQPDGTRMVS EGYSLENCCY
RGRVQGHPSS WVSLCACSGI RGLIVLSPER GYTLELGPGD LQRPVISRIQ DHLLLGHTCA
PSWHASVPTR AGPDLLLEQH HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT
LEAALLLDTF FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD
SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE LGHSLGLDHD
SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE KALLEGMGSC LFERQPSLAP
MSSLCGNMFV DPGEQCDCGF PDECTDPCCD HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL
CRPPTDDCDL PEFCPGDSSQ CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA
QPAAPLCLQT ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL
SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV DLLGAQECRR
KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL LSLLLLLVLV LLGASYWHRA
RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP QRAQQMTGTK QASVVSFPVP PSRPLPPNPV
PKKLQAALAD RSNPPTRPLP ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG
DGSLPLVVPS RPAPPPPAAS SLYL


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