CDCP1_HUMAN
ID CDCP1_HUMAN Reviewed; 836 AA.
AC Q9H5V8; Q49UB4; Q6NT71; Q6U9Y2; Q8WU91; Q96QU7; Q9H676; Q9H8C2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=CUB domain-containing protein 1;
DE AltName: Full=Membrane glycoprotein gp140;
DE AltName: Full=Subtractive immunization M plus HEp3-associated 135 kDa protein;
DE Short=SIMA135;
DE AltName: Full=Transmembrane and associated with src kinases;
DE AltName: CD_antigen=CD318;
DE Flags: Precursor;
GN Name=CDCP1; Synonyms=TRASK; ORFNames=UNQ2486/PRO5773;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT GLY-709.
RX PubMed=11466621; DOI=10.1038/sj.onc.1204566;
RA Scherl-Mostageer M., Sommergruber W., Abseher R., Hauptmann R., Ambros P.,
RA Schweifer N.;
RT "Identification of a novel gene, CDCP1, overexpressed in human colorectal
RT cancer.";
RL Oncogene 20:4402-4408(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-48; 281-293
RP AND 427-438, GLYCOSYLATION, PHOSPHORYLATION, SHEDDING, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND VARIANTS ARG-525 AND GLY-709.
RX PubMed=12660814; DOI=10.1038/sj.onc.1206220;
RA Hooper J.D., Zijlstra A., Aimes R.T., Liang H., Claassen G.F., Tarin D.,
RA Testa J.E., Quigley J.P.;
RT "Subtractive immunization using highly metastatic human tumor cells
RT identifies SIMA135/CDCP1, a 135 kDa cell surface phosphorylated
RT glycoprotein antigen.";
RL Oncogene 22:1783-1794(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-34 AND
RP 369-375, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION,
RP GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH CDH2; CDH3; SDC1; SDC4
RP AND ST14, AND FUNCTION.
RX PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL Oncogene 24:5333-5343(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ARG-525 AND GLY-709.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-697 (ISOFORM 1), AND VARIANT VAL-673.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-691 (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, PHOSPHORYLATION AT TYR-734, GLYCOSYLATION, TRYPTIC CLEAVAGE,
RP AND VARIANT ARG-525.
RC TISSUE=Epidermis;
RX PubMed=14739293; DOI=10.1074/jbc.m309678200;
RA Brown T.A., Yang T.M., Zaitsevskaia T., Xia Y., Dunn C.A., Sigle R.O.,
RA Knudsen B., Carter W.G.;
RT "Adhesion or plasmin regulates tyrosine phosphorylation of a novel membrane
RT glycoprotein p80/gp140/CUB domain-containing protein 1 in epithelia.";
RL J. Biol. Chem. 279:14772-14783(2004).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION.
RC TISSUE=Epidermis;
RX PubMed=8647901; DOI=10.1083/jcb.132.4.727;
RA Xia Y., Gil S.G., Carter W.G.;
RT "Anchorage mediated by integrin alpha6beta4 to laminin 5 (epiligrin)
RT regulates tyrosine phosphorylation of a membrane-associated 80-kD
RT protein.";
RL J. Cell Biol. 132:727-740(1996).
RN [10]
RP FUNCTION.
RX PubMed=12799299; DOI=10.1111/j.1749-6632.2003.tb03249.x;
RA Conze T., Lammers R., Kuci S., Scherl-Mostageer M., Schweifer N., Kanz L.,
RA Buehring H.-J.;
RT "CDCP1 is a novel marker for hematopoietic stem cells.";
RL Ann. N. Y. Acad. Sci. 996:222-226(2003).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15153610; DOI=10.1634/stemcells.22-3-334;
RA Buehring H.-J., Kuci S., Conze T., Rathke G., Bartolovic K., Gruenebach F.,
RA Scherl-Mostageer M., Bruemmendorf T.H., Schweifer N., Lammers R.;
RT "CDCP1 identifies a broad spectrum of normal and malignant stem/progenitor
RT cell subsets of hematopoietic and nonhematopoietic origin.";
RL Stem Cells 22:334-343(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SRC AND PRKCG, AND
RP MUTAGENESIS OF TYR-734 AND TYR-762.
RX PubMed=15851033; DOI=10.1016/j.cell.2005.02.019;
RA Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.;
RT "The C2 domain of PKCdelta is a phosphotyrosine binding domain.";
RL Cell 121:271-280(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=16404722; DOI=10.1002/pmic.200500180;
RA Andre M., Le Caer J.-P., Greco C., Planchon S., El Nemer W., Boucheix C.,
RA Rubinstein E., Chamot-Rooke J., Le Naour F.;
RT "Proteomic analysis of the tetraspanin web using LC-ESI-MS/MS and MALDI-
RT FTICR-MS.";
RL Proteomics 6:1437-1449(2006).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=17335815; DOI=10.1016/j.febslet.2007.02.025;
RA Perry S.E., Robinson P., Melcher A., Quirke P., Buehring H.-J., Cook G.P.,
RA Blair G.E.;
RT "Expression of the CUB domain containing protein 1 (CDCP1) gene in
RT colorectal tumour cells.";
RL FEBS Lett. 581:1137-1142(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in cell adhesion and cell matrix association.
CC May play a role in the regulation of anchorage versus migration or
CC proliferation versus differentiation via its phosphorylation. May be a
CC novel marker for leukemia diagnosis and for immature hematopoietic stem
CC cell subsets. Belongs to the tetraspanin web involved in tumor
CC progression and metastasis. {ECO:0000269|PubMed:11466621,
CC ECO:0000269|PubMed:12799299, ECO:0000269|PubMed:15153610,
CC ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:16404722,
CC ECO:0000269|PubMed:8647901}.
CC -!- SUBUNIT: Interacts with CDH2/N-cadherin, CDH3/P-cadherin,
CC SDC1/syndecan-1, SDC4/syndecan-4 and the serine protease ST14/MT-SP1.
CC Also interacts with SRC and PRKCG/protein kinase C gamma.
CC {ECO:0000269|PubMed:15851033, ECO:0000269|PubMed:16007225}.
CC -!- INTERACTION:
CC Q9H5V8; O00560: SDCBP; NbExp=6; IntAct=EBI-1019736, EBI-727004;
CC Q9H5V8; P12931: SRC; NbExp=3; IntAct=EBI-1019736, EBI-621482;
CC Q9H5V8; P07947: YES1; NbExp=2; IntAct=EBI-1019736, EBI-515331;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}. Note=Shedding may also lead to a
CC soluble peptide.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H5V8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H5V8-2; Sequence=VSP_017432;
CC Name=3;
CC IsoId=Q9H5V8-3; Sequence=VSP_017433, VSP_017434;
CC -!- TISSUE SPECIFICITY: Highly expressed in mitotic cells with low
CC expression during interphase. Detected at highest levels in skeletal
CC muscle and colon with lower levels in kidney, small intestine, placenta
CC and lung. Up-regulated in a number of human tumor cell lines, as well
CC as in colorectal cancer, breast carcinoma and lung cancer. Also
CC expressed in cells with phenotypes reminiscent of mesenchymal stem
CC cells and neural stem cells. {ECO:0000269|PubMed:11466621,
CC ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:15153610,
CC ECO:0000269|PubMed:16007225}.
CC -!- PTM: Phosphorylated on tyrosine by kinases of the SRC family such as
CC SRC and YES as well as by the protein kinase C gamma/PRKCG.
CC Dephosphorylated by phosphotyrosine phosphatases. Also phosphorylated
CC by suramin, a heparin analog. Tyrosine phosphorylated in response to
CC dissociation of integrin alpha-6 beta-4 from laminin-5.
CC {ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:14739293,
CC ECO:0000269|PubMed:16007225, ECO:0000269|PubMed:8647901}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12660814,
CC ECO:0000269|PubMed:14739293, ECO:0000269|PubMed:16007225}.
CC -!- PTM: A soluble form may also be produced by proteolytic cleavage at the
CC cell surface (shedding). Another peptide of 80 kDa (p80) is present in
CC cultured keratinocytes probably due to tryptic cleavage at an
CC unidentified site on its N-terminal side. Converted to p80 by plasmin,
CC a trypsin-like protease.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15388.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY026461; AAK02058.1; -; mRNA.
DR EMBL; AF468010; AAO33397.1; -; mRNA.
DR EMBL; AY167484; AAO34538.1; -; mRNA.
DR EMBL; AY358779; AAQ89139.1; -; mRNA.
DR EMBL; AK023834; BAB14695.1; -; mRNA.
DR EMBL; AK026187; BAB15388.1; ALT_INIT; mRNA.
DR EMBL; AK026622; BAB15511.1; -; mRNA.
DR EMBL; AC104165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021099; AAH21099.1; -; mRNA.
DR EMBL; BC069254; AAH69254.1; -; mRNA.
DR EMBL; AY375452; AAR21289.1; -; mRNA.
DR CCDS; CCDS2727.1; -. [Q9H5V8-1]
DR CCDS; CCDS46812.1; -. [Q9H5V8-3]
DR RefSeq; NP_073753.3; NM_022842.4. [Q9H5V8-1]
DR RefSeq; NP_835488.1; NM_178181.2. [Q9H5V8-3]
DR AlphaFoldDB; Q9H5V8; -.
DR BioGRID; 122336; 21.
DR CORUM; Q9H5V8; -.
DR DIP; DIP-33861N; -.
DR IntAct; Q9H5V8; 26.
DR MINT; Q9H5V8; -.
DR STRING; 9606.ENSP00000296129; -.
DR GlyConnect; 1160; 13 N-Linked glycans (8 sites).
DR GlyGen; Q9H5V8; 10 sites, 12 N-linked glycans (8 sites).
DR iPTMnet; Q9H5V8; -.
DR PhosphoSitePlus; Q9H5V8; -.
DR SwissPalm; Q9H5V8; -.
DR BioMuta; CDCP1; -.
DR DMDM; 317373455; -.
DR CPTAC; CPTAC-2211; -.
DR EPD; Q9H5V8; -.
DR jPOST; Q9H5V8; -.
DR MassIVE; Q9H5V8; -.
DR MaxQB; Q9H5V8; -.
DR PaxDb; Q9H5V8; -.
DR PeptideAtlas; Q9H5V8; -.
DR PRIDE; Q9H5V8; -.
DR ProteomicsDB; 80933; -. [Q9H5V8-1]
DR ProteomicsDB; 80934; -. [Q9H5V8-2]
DR ProteomicsDB; 80935; -. [Q9H5V8-3]
DR ABCD; Q9H5V8; 13 sequenced antibodies.
DR Antibodypedia; 2564; 843 antibodies from 44 providers.
DR DNASU; 64866; -.
DR Ensembl; ENST00000296129.6; ENSP00000296129.1; ENSG00000163814.8. [Q9H5V8-1]
DR Ensembl; ENST00000425231.2; ENSP00000399342.2; ENSG00000163814.8. [Q9H5V8-3]
DR GeneID; 64866; -.
DR KEGG; hsa:64866; -.
DR MANE-Select; ENST00000296129.6; ENSP00000296129.1; NM_022842.5; NP_073753.3.
DR UCSC; uc003com.5; human. [Q9H5V8-1]
DR CTD; 64866; -.
DR DisGeNET; 64866; -.
DR GeneCards; CDCP1; -.
DR HGNC; HGNC:24357; CDCP1.
DR HPA; ENSG00000163814; Tissue enhanced (esophagus).
DR MIM; 611735; gene.
DR neXtProt; NX_Q9H5V8; -.
DR OpenTargets; ENSG00000163814; -.
DR PharmGKB; PA142672140; -.
DR VEuPathDB; HostDB:ENSG00000163814; -.
DR eggNOG; ENOG502QVKN; Eukaryota.
DR GeneTree; ENSGT00390000010209; -.
DR HOGENOM; CLU_007498_0_0_1; -.
DR InParanoid; Q9H5V8; -.
DR OMA; RFVPGCF; -.
DR OrthoDB; 223122at2759; -.
DR PhylomeDB; Q9H5V8; -.
DR TreeFam; TF331392; -.
DR PathwayCommons; Q9H5V8; -.
DR SignaLink; Q9H5V8; -.
DR SIGNOR; Q9H5V8; -.
DR BioGRID-ORCS; 64866; 9 hits in 1082 CRISPR screens.
DR ChiTaRS; CDCP1; human.
DR GeneWiki; CDCP1; -.
DR GenomeRNAi; 64866; -.
DR Pharos; Q9H5V8; Tbio.
DR PRO; PR:Q9H5V8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H5V8; protein.
DR Bgee; ENSG00000163814; Expressed in gingival epithelium and 133 other tissues.
DR Genevisible; Q9H5V8; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR038811; CDCP1.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR14477; PTHR14477; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:12660814,
FT ECO:0000269|PubMed:16007225"
FT CHAIN 30..836
FT /note="CUB domain-containing protein 1"
FT /id="PRO_0000226249"
FT TOPO_DOM 30..667
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 417..544
FT /note="CUB"
FT REGION 776..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 368..369
FT /note="Cleavage; by ST14/MT-SP1"
FT MOD_RES 734
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:14739293"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 476..499
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017432"
FT VAR_SEQ 342..343
FT /note="NK -> SE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017433"
FT VAR_SEQ 344..836
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017434"
FT VARIANT 525
FT /note="Q -> R (in dbSNP:rs3749191)"
FT /evidence="ECO:0000269|PubMed:12660814,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:14739293"
FT /id="VAR_025498"
FT VARIANT 673
FT /note="A -> V (in dbSNP:rs35428731)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055095"
FT VARIANT 709
FT /note="D -> G (in dbSNP:rs9874077)"
FT /evidence="ECO:0000269|PubMed:11466621,
FT ECO:0000269|PubMed:12660814, ECO:0000269|PubMed:14702039"
FT /id="VAR_025499"
FT MUTAGEN 734
FT /note="Y->F: Impaired association with SRC."
FT /evidence="ECO:0000269|PubMed:15851033"
FT MUTAGEN 762
FT /note="Y->F: Impaired association with protein kinase PRKCG
FT but not with SRC."
FT /evidence="ECO:0000269|PubMed:15851033"
FT CONFLICT 252
FT /note="W -> C (in Ref. 5; BAB14695)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Y -> D (in Ref. 5; BAB15388)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="S -> G (in Ref. 5; BAB14695)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="K -> R (in Ref. 5; BAB15388)"
FT /evidence="ECO:0000305"
FT CONFLICT 827
FT /note="N -> S (in Ref. 2; AAO33397 and 5; BAB15511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 92932 MW; 544FFDBBDD371518 CRC64;
MAGLNCGVSI ALLGVLLLGA ARLPRGAEAF EIALPRESNI TVLIKLGTPT LLAKPCYIVI
SKRHITMLSI KSGERIVFTF SCQSPENHFV IEIQKNIDCM SGPCPFGEVQ LQPSTSLLPT
LNRTFIWDVK AHKSIGLELQ FSIPRLRQIG PGESCPDGVT HSISGRIDAT VVRIGTFCSN
GTVSRIKMQE GVKMALHLPW FHPRNVSGFS IANRSSIKRL CIIESVFEGE GSATLMSANY
PEGFPEDELM TWQFVVPAHL RASVSFLNFN LSNCERKEER VEYYIPGSTT NPEVFKLEDK
QPGNMAGNFN LSLQGCDQDA QSPGILRLQF QVLVQHPQNE SNKIYVVDLS NERAMSLTIE
PRPVKQSRKF VPGCFVCLES RTCSSNLTLT SGSKHKISFL CDDLTRLWMN VEKTISCTDH
RYCQRKSYSL QVPSDILHLP VELHDFSWKL LVPKDRLSLV LVPAQKLQQH THEKPCNTSF
SYLVASAIPS QDLYFGSFCP GGSIKQIQVK QNISVTLRTF APSFQQEASR QGLTVSFIPY
FKEEGVFTVT PDTKSKVYLR TPNWDRGLPS LTSVSWNISV PRDQVACLTF FKERSGVVCQ
TGRAFMIIQE QRTRAEEIFS LDEDVLPKPS FHHHSFWVNI SNCSPTSGKQ LDLLFSVTLT
PRTVDLTVIL IAAVGGGVLL LSALGLIICC VKKKKKKTNK GPAVGIYNDN INTEMPRQPK
KFQKGRKDND SHVYAVIEDT MVYGHLLQDS SGSFLQPEVD TYRPFQGTMG VCPPSPPTIC
SRAPTAKLAT EEPPPRSPPE SESEPYTFSH PNNGDVSSKD TDIPLLNTQE PMEPAE
