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Extracellular matrix protein 1 (Secretory component p85)

 ECM1_HUMAN              Reviewed;         540 AA.
Q16610; A8K8S0; B4DW49; B4DY60; O43266; Q5T5G4; Q5T5G5; Q5T5G6;
Q8IZ60;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
28-MAR-2018, entry version 155.
RecName: Full=Extracellular matrix protein 1;
AltName: Full=Secretory component p85;
Flags: Precursor;
Name=ECM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
VARIANT SER-415.
PubMed=9367673; DOI=10.1006/geno.1997.4918;
Smits P., Ni J., Feng P., Wauters J., van Hul W., Boutaibi M.E.,
Dillon P.J., Merregaert J.;
"The human extracellular matrix gene 1 (ECM1): genomic structure, cDNA
cloning, expression pattern, and chromosomal localization.";
Genomics 45:487-495(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=9501329; DOI=10.1016/S0945-053X(97)90017-2;
Johnson M.R., Wilkin D.J., Vos H.L., Ortiz de Luna R.I., Dehejia A.M.,
Polymeropoulos M.H., Francomano C.A.;
"Characterization of the human extracellular matrix protein 1 gene on
chromosome 1q21.";
Matrix Biol. 16:289-292(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
VARIANTS MET-130 AND SER-415.
TISSUE=Synovial cell, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
MET-130 AND SER-415.
TISSUE=Skin;
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).
[7]
FUNCTION IN BONE FORMATION.
PubMed=11165938; DOI=10.1016/S8756-3282(00)00428-2;
Deckers M.M.L., Smits P., Karperien M., Ni J., Tylzanowski P.,
Feng P., Parmelee D., Zhang J., Bouffard E., Gentz R.,
Loewik C.W.G.M., Merregaert J.;
"Recombinant human extracellular matrix protein 1 inhibits alkaline
phosphatase activity and mineralization of mouse embryonic metatarsals
in vitro.";
Bone 28:14-20(2001).
[8]
FUNCTION IN ANGIOGENESIS, AND TISSUE SPECIFICITY.
PubMed=11292659; DOI=10.1096/fj.99-0934com;
Han Z., Ni J., Smits P., Underhill C.B., Xie B., Chen Y., Liu N.,
Tylzanowski P., Parmelee D., Feng P., Ding I., Gao F., Gentz R.,
Huylebroeck D., Merregaert J., Zhang L.;
"Extracellular matrix protein 1 (ECM1) has angiogenic properties and
is expressed by breast tumor cells.";
FASEB J. 15:988-994(2001).
[9]
INVOLVEMENT IN LIPOID PROTEINOSIS.
PubMed=11929856; DOI=10.1093/hmg/11.7.833;
Hamada T., McLean W.H.I., Ramsay M., Ashton G.H.S., Nanda A.,
Jenkins T., Edelstein I., South A.P., Bleck O., Wessagowit V.,
Mallipeddi R., Orchard G.E., Wan H., Dopping-Hepenstal P.J.C.,
Mellerio J.E., Whittock N.V., Munro C.S., van Steensel M.A.M.,
Steijlen P.M., Ni J., Zhang L., Hashimoto T., Eady R.A.E.,
McGrath J.A.;
"Lipoid proteinosis maps to 1q21 and is caused by mutations in the
extracellular matrix protein 1 gene (ECM1).";
Hum. Mol. Genet. 11:833-840(2002).
[10]
INTERACTION WITH HSPG2, AND TISSUE SPECIFICITY.
PubMed=12604605; DOI=10.1074/jbc.M210529200;
Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V.;
"Perlecan protein core interacts with extracellular matrix protein 1
(ECM1), a glycoprotein involved in bone formation and angiogenesis.";
J. Biol. Chem. 278:17491-17499(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-444.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
INTERACTION WITH MMP9, AND FUNCTION.
PubMed=16512877; DOI=10.1111/j.0906-6705.2006.00409.x;
Fujimoto N., Terlizzi J., Aho S., Brittingham R., Fertala A.,
Oyama N., McGrath J.A., Uitto J.;
"Extracellular matrix protein 1 inhibits the activity of matrix
metalloproteinase 9 through high-affinity protein/protein
interactions.";
Exp. Dermatol. 15:300-307(2006).
[13]
INTERACTION WITH EFEMP1 AND LAMB3.
PubMed=19275936; DOI=10.1016/j.matbio.2009.02.003;
Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A.,
Geentjens K., Sasaki T., Oyama N., Merregaert J.;
"ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332
through its serum albumin subdomain-like 2 domain.";
Matrix Biol. 28:160-169(2009).
[14]
GLYCOSYLATION AT ASN-444.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
VARIANT LIP ILE-167, AND VARIANTS MET-130 AND SER-415.
PubMed=12603844; DOI=10.1046/j.1523-1747.2003.12073.x;
Hamada T., Wessagowit V., South A.P., Ashton G.H.S., Chan I.,
Oyama N., Siriwattana A., Jewhasuchin P., Charuwichitratana S.,
Thappa D.M., Lenane P., Krafchik B., Kulthanan K., Shimizu H.,
Kaya T.I., Erdal M.E., Paradisi M., Paller A.S., Seishima M.,
Hashimoto T., McGrath J.A.;
"Extracellular matrix protein 1 gene (ECM1) mutations in lipoid
proteinosis and genotype-phenotype correlation.";
J. Invest. Dermatol. 120:345-350(2003).
-!- FUNCTION: Involved in endochondral bone formation as negative
regulator of bone mineralization. Stimulates the proliferation of
endothelial cells and promotes angiogenesis. Inhibits MMP9
proteolytic activity. {ECO:0000269|PubMed:11165938,
ECO:0000269|PubMed:11292659, ECO:0000269|PubMed:16512877}.
-!- SUBUNIT: Interacts (via C-terminus) with HSPG2 (via C-terminus).
Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9.
{ECO:0000269|PubMed:12604605, ECO:0000269|PubMed:16512877,
ECO:0000269|PubMed:19275936}.
-!- INTERACTION:
O75934:BCAS2; NbExp=4; IntAct=EBI-947964, EBI-1050106;
P09234:SNRPC; NbExp=4; IntAct=EBI-947964, EBI-766589;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=1a;
IsoId=Q16610-1; Sequence=Displayed;
Name=2; Synonyms=1b;
IsoId=Q16610-2; Sequence=VSP_036414;
Name=3;
IsoId=Q16610-3; Sequence=VSP_036411, VSP_036412, VSP_036415,
VSP_036416;
Name=4;
IsoId=Q16610-4; Sequence=VSP_036413;
Note=May be due to intron retention.;
-!- TISSUE SPECIFICITY: Expressed in breast cancer tissues. Little or
no expression observed in normal breast tissues. Expressed in
skin; wide expression is observed throughout the dermis with
minimal expression in the epidermis. {ECO:0000269|PubMed:11292659,
ECO:0000269|PubMed:12604605}.
-!- DISEASE: Lipoid proteinosis (LiP) [MIM:247100]: Rare autosomal
recessive disorder characterized by generalized thickening of
skin, mucosae and certain viscera. Classical features include
beaded eyelid papules and laryngeal infiltration leading to
hoarseness. Histologically, there is widespread deposition of
hyaline material and disruption/reduplication of basement
membrane. {ECO:0000269|PubMed:11929856,
ECO:0000269|PubMed:12603844}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ECM1ID40398ch1q21.html";
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EMBL; U68186; AAB88081.1; -; mRNA.
EMBL; U68187; AAB88082.1; -; mRNA.
EMBL; U65932; AAB05933.1; -; mRNA.
EMBL; U65938; AAB05934.1; -; Genomic_DNA.
EMBL; U65933; AAB05934.1; JOINED; Genomic_DNA.
EMBL; U65934; AAB05934.1; JOINED; Genomic_DNA.
EMBL; U65935; AAB05934.1; JOINED; Genomic_DNA.
EMBL; U65936; AAB05934.1; JOINED; Genomic_DNA.
EMBL; U65937; AAB05934.1; JOINED; Genomic_DNA.
EMBL; AK097046; BAG53412.1; -; mRNA.
EMBL; AK292435; BAF85124.1; -; mRNA.
EMBL; AK301369; BAG62911.1; -; mRNA.
EMBL; AK302279; BAG63622.1; -; mRNA.
EMBL; AL356356; CAI15491.1; -; Genomic_DNA.
EMBL; AL356356; CAI15492.1; -; Genomic_DNA.
EMBL; AL356356; CAI15493.1; -; Genomic_DNA.
EMBL; CH471121; EAW53544.1; -; Genomic_DNA.
EMBL; CH471121; EAW53545.1; -; Genomic_DNA.
EMBL; CH471121; EAW53546.1; -; Genomic_DNA.
EMBL; BC023505; AAH23505.1; -; mRNA.
CCDS; CCDS55632.1; -. [Q16610-4]
CCDS; CCDS953.1; -. [Q16610-1]
CCDS; CCDS954.1; -. [Q16610-2]
RefSeq; NP_001189787.1; NM_001202858.1. [Q16610-4]
RefSeq; NP_004416.2; NM_004425.3. [Q16610-1]
RefSeq; NP_073155.2; NM_022664.2. [Q16610-2]
UniGene; Hs.81071; -.
ProteinModelPortal; Q16610; -.
BioGrid; 108222; 31.
IntAct; Q16610; 31.
STRING; 9606.ENSP00000358045; -.
iPTMnet; Q16610; -.
PhosphoSitePlus; Q16610; -.
BioMuta; ECM1; -.
DMDM; 48429255; -.
MaxQB; Q16610; -.
PaxDb; Q16610; -.
PeptideAtlas; Q16610; -.
PRIDE; Q16610; -.
DNASU; 1893; -.
Ensembl; ENST00000346569; ENSP00000271630; ENSG00000143369. [Q16610-2]
Ensembl; ENST00000369047; ENSP00000358043; ENSG00000143369. [Q16610-1]
Ensembl; ENST00000369049; ENSP00000358045; ENSG00000143369. [Q16610-4]
GeneID; 1893; -.
KEGG; hsa:1893; -.
UCSC; uc001eus.4; human. [Q16610-1]
CTD; 1893; -.
DisGeNET; 1893; -.
EuPathDB; HostDB:ENSG00000143369.14; -.
GeneCards; ECM1; -.
HGNC; HGNC:3153; ECM1.
HPA; HPA027241; -.
MalaCards; ECM1; -.
MIM; 247100; phenotype.
MIM; 602201; gene.
neXtProt; NX_Q16610; -.
OpenTargets; ENSG00000143369; -.
Orphanet; 530; Lipoid proteinosis.
PharmGKB; PA27598; -.
eggNOG; ENOG410IVN8; Eukaryota.
eggNOG; ENOG4111TGN; LUCA.
GeneTree; ENSGT00390000006215; -.
HOVERGEN; HBG005561; -.
InParanoid; Q16610; -.
OMA; CCHYPPS; -.
OrthoDB; EOG091G0NAE; -.
PhylomeDB; Q16610; -.
TreeFam; TF330786; -.
Reactome; R-HSA-114608; Platelet degranulation.
SIGNOR; Q16610; -.
ChiTaRS; ECM1; human.
GeneWiki; ECM1; -.
GenomeRNAi; 1893; -.
PRO; PR:Q16610; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143369; -.
CleanEx; HS_ECM1; -.
ExpressionAtlas; Q16610; baseline and differential.
Genevisible; Q16610; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005134; F:interleukin-2 receptor binding; IEA:Ensembl.
GO; GO:0043236; F:laminin binding; IPI:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; HMP:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:2000404; P:regulation of T cell migration; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0002828; P:regulation of type 2 immune response; IEA:Ensembl.
InterPro; IPR008605; ECM1.
InterPro; IPR020858; Serum_albumin-like.
PANTHER; PTHR16776; PTHR16776; 1.
Pfam; PF05782; ECM1; 1.
SUPFAM; SSF48552; SSF48552; 2.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Biomineralization;
Complete proteome; Disease mutation; Extracellular matrix;
Glycoprotein; Mineral balance; Osteogenesis; Polymorphism;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 19 {ECO:0000250|UniProtKB:Q62894}.
CHAIN 20 540 Extracellular matrix protein 1.
/FTId=PRO_0000021146.
REPEAT 150 279 1.
REPEAT 283 405 2.
REGION 150 405 2 X approximate repeats.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 71 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036411.
VAR_SEQ 72 81 QSQVQPPPSQ -> MALPLRDRVK (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036412.
VAR_SEQ 74 74 Q -> GKEGRGPRPHSQPWLGERVGCSHIPPSI (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036413.
VAR_SEQ 237 361 Missing (in isoform 2).
{ECO:0000303|PubMed:9367673}.
/FTId=VSP_036414.
VAR_SEQ 237 241 WEEAM -> VRLGS (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036415.
VAR_SEQ 242 540 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036416.
VARIANT 130 130 T -> M (in dbSNP:rs3737240).
{ECO:0000269|PubMed:12603844,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_018690.
VARIANT 167 167 F -> I (in LiP; dbSNP:rs121909116).
{ECO:0000269|PubMed:12603844}.
/FTId=VAR_018691.
VARIANT 415 415 G -> S (in dbSNP:rs13294).
{ECO:0000269|PubMed:12603844,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9367673}.
/FTId=VAR_014761.
VARIANT 528 528 G -> R (in dbSNP:rs1050901).
/FTId=VAR_014762.
VARIANT 535 535 S -> F (in dbSNP:rs1050904).
/FTId=VAR_014763.
CONFLICT 78 84 Missing (in Ref. 3; BAG63622).
{ECO:0000305}.
CONFLICT 520 520 Q -> R (in Ref. 3; BAF85124).
{ECO:0000305}.
SEQUENCE 540 AA; 60674 MW; EA575895CDE068BE CRC64;
MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP LSRSLPMDHP
DSSQHGPPFE GQSQVQPPPS QEATPLQQEK LLPAQLPAEK EVGPPLPQEA VPLQKELPSL
QHPNEQKEGT PAPFGDQSHP EPESWNAAQH CQQDRSQGGW GHRLDGFPPG RPSPDNLNQI
CLPNRQHVVY GPWNLPQSSY SHLTRQGETL NFLEIGYSRC CHCRSHTNRL ECAKLVWEEA
MSRFCEAEFS VKTRPHWCCT RQGEARFSCF QEEAPQPHYQ LRACPSHQPD ISSGLELPFP
PGVPTLDNIK NICHLRRFRS VPRNLPATDP LQRELLALIQ LEREFQRCCR QGNNHTCTWK
AWEDTLDKYC DREYAVKTHH HLCCRHPPSP TRDECFARRA PYPNYDRDIL TIDIGRVTPN
LMGHLCGNQR VLTKHKHIPG LIHNMTARCC DLPFPEQACC AEEEKLTFIN DLCGPRRNIW
RDPALCCYLS PGDEQVNCFN INYLRNVALV SGDTENAKGQ GEQGSTGGTN ISSTSEPKEE


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