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Platelet endothelial cell adhesion molecule (PECAM-1) (CD antigen CD31)

 PECA1_MOUSE             Reviewed;         727 AA.
Q08481; B1ARB1; B1ARB2; Q3TES6; Q922E0;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
07-NOV-2018, entry version 166.
RecName: Full=Platelet endothelial cell adhesion molecule;
Short=PECAM-1;
AltName: CD_antigen=CD31;
Flags: Precursor;
Name=Pecam1; Synonyms=Pecam, Pecam-1;
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 1).
STRAIN=BALB/cJ; TISSUE=Lung;
PubMed=8516303; DOI=10.1073/pnas.90.12.5569;
Xie Y., Muller W.A.;
"Molecular cloning and adhesive properties of murine
platelet/endothelial cell adhesion molecule 1.";
Proc. Natl. Acad. Sci. U.S.A. 90:5569-5573(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Stomach;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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).
[6]
PROTEIN SEQUENCE OF 18-26.
TISSUE=Heart;
PubMed=1415479;
Bogen S.A., Baldwin H.S., Watkins S.C., Albelda S.M., Abbas A.K.;
"Association of murine CD31 with transmigrating lymphocytes following
antigenic stimulation.";
Am. J. Pathol. 141:843-854(1992).
[7]
PHOSPHORYLATION AT TYR-679 AND TYR-702 BY FES AND FER, AND MUTAGENESIS
OF TYR-679; TYR-702 AND TYR-717.
PubMed=16731527; DOI=10.1074/jbc.M604252200;
Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.;
"Fer and Fps/Fes participate in a Lyn-dependent pathway from
FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit
mast cell activation.";
J. Biol. Chem. 281:20949-20957(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-702, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19048083; DOI=10.1242/dmm.000547;
Stevens H.Y., Melchior B., Bell K.S., Yun S., Yeh J.C., Frangos J.A.;
"PECAM-1 is a critical mediator of atherosclerosis.";
Dis. Model. Mech. 1:175-181(2008).
[10]
ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
PubMed=18388311; DOI=10.1242/jcs.025163;
Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J.;
"An alternatively spliced isoform of PECAM-1 is expressed at high
levels in human and murine tissues, and suggests a novel role for the
C-terminus of PECAM-1 in cytoprotective signaling.";
J. Cell Sci. 121:1235-1242(2008).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-141; ASN-360;
ASN-424 AND ASN-540.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Cell adhesion molecule which is required for leukocyte
transendothelial migration (TEM) under most inflammatory
conditions (By similarity). Tyr-679 plays a critical role in TEM
and is required for efficient trafficking of PECAM1 to and from
the lateral border recycling compartment (LBRC) and is also
essential for the LBRC membrane to be targeted around migrating
leukocytes (By similarity). Trans-homophilic interaction may play
a role in endothelial cell-cell adhesion via cell junctions (By
similarity). Heterophilic interaction with CD177 plays a role in
transendothelial migration of neutrophils (By similarity).
Homophilic ligation of PECAM1 prevents macrophage-mediated
phagocytosis of neighboring viable leukocytes by transmitting a
detachment signal (By similarity). Promotes macrophage-mediated
phagocytosis of apoptotic leukocytes by tethering them to the
phagocytic cells; PECAM1-mediated detachment signal appears to be
disabled in apoptotic leukocytes (By similarity). Modulates
bradykinin receptor BDKRB2 activation (By similarity). Regulates
bradykinin- and hyperosmotic shock-induced ERK1/2 activation in
endothelial cells (By similarity). Induces susceptibility to
atherosclerosis (PubMed:19048083). {ECO:0000250|UniProtKB:P16284,
ECO:0000269|PubMed:19048083}.
-!- SUBUNIT: Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-
type 2 domains); trans-homodimerization is required for cell-cell
interaction. Forms a complex with BDKRB2 and GNAQ. Interacts with
BDKRB2 and GNAQ. Interacts with PTPN11; Tyr-702 is critical for
PTPN11 recruitment. Interacts with FER. Interacts with CD177; the
interaction is Ca(2+)-dependent; the interaction is direct.
{ECO:0000250|UniProtKB:P16284, ECO:0000250|UniProtKB:P51866}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P16284}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P16284}. Membrane raft
{ECO:0000250|UniProtKB:P16284}. Cell junction
{ECO:0000250|UniProtKB:P16284}. Note=Localizes to the lateral
border recycling compartment (LBRC) and recycles from the LBRC to
the junction in resting endothelial cells. Cell surface expression
on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated
stimulation. {ECO:0000250|UniProtKB:P16284}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q08481-1; Sequence=Displayed;
Name=2;
IsoId=Q08481-2; Sequence=VSP_038724;
Name=3;
IsoId=Q08481-3; Sequence=VSP_038725;
Name=4;
IsoId=Q08481-4; Sequence=VSP_038723;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in lung
and platelets. {ECO:0000269|PubMed:18388311}.
-!- DOMAIN: The Ig-like C2-type domains 2 and 3 contribute to
formation of the complex with BDKRB2 and in regulation of its
activity. {ECO:0000250}.
-!- PTM: Phosphorylated on Ser and Tyr residues by src kinases after
cellular activation (PubMed:16731527). Upon activation,
phosphorylated on Ser-718 which probably initiates the
dissociation of the membrane-interaction segment (residues 698-
718) from the cell membrane allowing the sequential
phosphorylation of Tyr-702 and Tyr-679 (By similarity).
Constitutively phosphorylated on Ser-723 in resting platelets (By
similarity). Phosphorylated on tyrosine residues by FER and FES in
response to FCER1 activation (PubMed:16731527). In endothelial
cells Fyn mediates mechanical-force (stretch or pull) induced
tyrosine phosphorylation (By similarity).
{ECO:0000250|UniProtKB:P16284, ECO:0000269|PubMed:16731527}.
-!- PTM: Palmitoylation by ZDHHC21 is necessary for cell surface
expression in endothelial cells and enrichment in membrane rafts.
{ECO:0000250|UniProtKB:P16284}.
-!- DISRUPTION PHENOTYPE: Mice show reduced atherosclerotic lesions.
There is down-regulation of ICAM-1 in endothelial cells at the
lesion periphery, and reduced disruption of Cx43 junctional
staining at arterial branch points and in the descending aorta.
{ECO:0000269|PubMed:19048083}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=PECAM-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_191";
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EMBL; L06039; AAA16230.1; -; mRNA.
EMBL; AK169431; BAE41172.1; -; mRNA.
EMBL; AL603664; CAM18558.1; -; Genomic_DNA.
EMBL; AL603664; CAM18559.1; -; Genomic_DNA.
EMBL; AL603664; CAM18560.1; -; Genomic_DNA.
EMBL; CH466558; EDL34303.1; -; Genomic_DNA.
EMBL; CH466558; EDL34304.1; -; Genomic_DNA.
EMBL; CH466558; EDL34305.1; -; Genomic_DNA.
EMBL; BC008519; AAH08519.1; -; mRNA.
EMBL; BC085502; AAH85502.1; -; mRNA.
CCDS; CCDS25558.1; -. [Q08481-2]
CCDS; CCDS25559.1; -. [Q08481-3]
CCDS; CCDS79068.1; -. [Q08481-4]
CCDS; CCDS79069.1; -. [Q08481-1]
RefSeq; NP_001027550.1; NM_001032378.2. [Q08481-2]
RefSeq; NP_001292086.1; NM_001305157.1. [Q08481-1]
RefSeq; NP_001292087.1; NM_001305158.1. [Q08481-4]
RefSeq; NP_032842.2; NM_008816.3. [Q08481-3]
RefSeq; XP_011247094.1; XM_011248792.1. [Q08481-1]
UniGene; Mm.343951; -.
ProteinModelPortal; Q08481; -.
SMR; Q08481; -.
IntAct; Q08481; 5.
MINT; Q08481; -.
STRING; 10090.ENSMUSP00000079664; -.
iPTMnet; Q08481; -.
PhosphoSitePlus; Q08481; -.
SwissPalm; Q08481; -.
MaxQB; Q08481; -.
PaxDb; Q08481; -.
PeptideAtlas; Q08481; -.
PRIDE; Q08481; -.
Ensembl; ENSMUST00000080853; ENSMUSP00000079664; ENSMUSG00000020717. [Q08481-3]
Ensembl; ENSMUST00000103069; ENSMUSP00000099358; ENSMUSG00000020717. [Q08481-2]
Ensembl; ENSMUST00000106796; ENSMUSP00000102408; ENSMUSG00000020717. [Q08481-1]
Ensembl; ENSMUST00000183610; ENSMUSP00000138959; ENSMUSG00000020717. [Q08481-4]
GeneID; 18613; -.
KEGG; mmu:18613; -.
UCSC; uc007lze.2; mouse. [Q08481-1]
UCSC; uc007lzf.2; mouse. [Q08481-3]
UCSC; uc007lzg.2; mouse. [Q08481-2]
UCSC; uc007lzh.2; mouse. [Q08481-4]
CTD; 5175; -.
MGI; MGI:97537; Pecam1.
eggNOG; ENOG410II37; Eukaryota.
eggNOG; ENOG4111F9A; LUCA.
GeneTree; ENSGT00440000034155; -.
HOGENOM; HOG000049132; -.
HOVERGEN; HBG059434; -.
InParanoid; Q08481; -.
KO; K06471; -.
OMA; YTCKVEA; -.
TreeFam; TF338229; -.
ChiTaRS; Pecam1; mouse.
PRO; PR:Q08481; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020717; Expressed in 189 organ(s), highest expression level in embryo mesenchyme (mouse).
CleanEx; MM_PECAM1; -.
ExpressionAtlas; Q08481; baseline and differential.
Genevisible; Q08481; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0001726; C:ruffle; ISO:MGI.
GO; GO:0030485; C:smooth muscle contractile fiber; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISO:MGI.
GO; GO:0050904; P:diapedesis; ISO:MGI.
GO; GO:0043542; P:endothelial cell migration; IDA:MGI.
GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
GO; GO:0090673; P:endothelial cell-matrix adhesion; IMP:MGI.
GO; GO:0072011; P:glomerular endothelium development; IEA:Ensembl.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0072672; P:neutrophil extravasation; ISO:MGI.
GO; GO:0006909; P:phagocytosis; ISO:MGI.
GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:MGI.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
GO; GO:0042060; P:wound healing; IMP:MGI.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 17 {ECO:0000269|PubMed:1415479}.
CHAIN 18 727 Platelet endothelial cell adhesion
molecule.
/FTId=PRO_0000014896.
TOPO_DOM 18 590 Extracellular. {ECO:0000255}.
TRANSMEM 591 609 Helical. {ECO:0000255}.
TOPO_DOM 610 727 Cytoplasmic. {ECO:0000255}.
DOMAIN 40 126 Ig-like C2-type 1.
DOMAIN 135 213 Ig-like C2-type 2.
DOMAIN 225 309 Ig-like C2-type 3.
DOMAIN 315 391 Ig-like C2-type 4.
DOMAIN 413 472 Ig-like C2-type 5.
DOMAIN 488 578 Ig-like C2-type 6.
REGION 698 718 Membrane-bound segment which detaches
upon phosphorylation.
{ECO:0000250|UniProtKB:P16284}.
REGION 710 727 May play a role in cytoprotective
signaling. {ECO:0000250}.
MOTIF 677 682 ITIM motif 1.
{ECO:0000250|UniProtKB:P16284}.
MOTIF 700 705 ITIM motif 2.
{ECO:0000250|UniProtKB:P16284}.
MOD_RES 679 679 Phosphotyrosine; by FER.
{ECO:0000305|PubMed:16731527}.
MOD_RES 702 702 Phosphotyrosine; by FER.
{ECO:0000244|PubMed:17947660,
ECO:0000269|PubMed:16731527}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000250|UniProtKB:P16284}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000250|UniProtKB:P16284}.
LIPID 611 611 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 360 360 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 540 540 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 47 99 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 142 195 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 245 293 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 336 375 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 420 465 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 512 561 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 119 219 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038723.
VAR_SEQ 692 727 ALGTRATETVYSEIRKVDPNLMENRYSRTEGSLNGT -> E
NGRLP (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038724.
VAR_SEQ 711 727 NLMENRYSRTEGSLNGT -> KNGRLP (in isoform
3). {ECO:0000305}.
/FTId=VSP_038725.
MUTAGEN 679 679 Y->F: Reduces tyrosine phosphorylation by
FER by about 60%.
{ECO:0000269|PubMed:16731527}.
MUTAGEN 702 702 Y->F: Reduces tyrosine phosphorylation by
FER by about 60%.
{ECO:0000269|PubMed:16731527}.
MUTAGEN 717 717 Y->F: No significant effect on
phosphorylation by FER.
{ECO:0000269|PubMed:16731527}.
CONFLICT 18 18 E -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 727 AA; 81263 MW; 34C04752D199BAA5 CRC64;
MLLALGLTLV LYASLQAEEN SFTINSIHME SLPSWEVMNG QQLTLECLVD ISTTSKSRSQ
HRVLFYKDDA MVYNVTSREH TESYVIPQAR VFHSGKYKCT VMLNNKEKTT IEYEVKVHGV
SKPKVTLDKK EVTEGGVVTV NCSLQEEKPP IFFKIEKLEV GTKFVKRRID KTSNENFVLM
EFPIEAQDHV LVFRCQAGIL SGFKLQESEP IRSEYVTVQE SFSTPKFEIK PPGMIIEGDQ
LHIRCIVQVT HLVQEFTEII IQKDKAIVAT SKQSSEAVYS VMAMVEYSGH YTCKVESNRI
SKASSIMVNI TELFPKPKLE FSSSRLDQGE LLDLSCSVSG TPVANFTIQK EETVLSQYQN
FSKIAEESDS GEYSCTAGIG KVVKRSGLVP IQVCEMLSKP SIFHDAKSEI IKGHAIGISC
QSENGTAPIT YHLMKAKSDF QTLEVTSNDP ATFTDKPTRD MEYQCRADNC HSHPAVFSEI
LRVRVIAPVD EVVISILSSN EVQSGSEMVL RCSVKEGTSP ITFQFYKEKE DRPFHQAVVN
DTQAFWHNKQ ASKKQEGQYY CTASNRASSM RTSPRSSTLA VRVFLAPWKK GLIAVVVIGV
VIATLIVAAK CYFLRKAKAK QKPVEMSRPA APLLNSNSEK ISEPSVEANS HYGYDDVSGN
DAVKPINQNK DPQNMDVEYT EVEVSSLEPH QALGTRATET VYSEIRKVDP NLMENRYSRT
EGSLNGT


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