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Database: UniProt
Entry: Q8IWY4
LinkDB: Q8IWY4
Original site: Q8IWY4 
ID   SCUB1_HUMAN             Reviewed;         988 AA.
AC   Q8IWY4; Q5R336;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   13-FEB-2019, entry version 130.
DE   RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=SCUBE1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-398 AND PRO-648, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=12270931; DOI=10.1074/jbc.M207410200;
RA   Yang R.-B., Ng C.K.D., Wasserman S.M., Colman S.D., Shenoy S.,
RA   Mehraban F., Koemueves L.G., Tomlinson J.E., Topper J.N.;
RT   "Identification of a novel family of cell-surface proteins expressed
RT   in human vascular endothelium.";
RL   J. Biol. Chem. 277:46364-46373(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16753137; DOI=10.1016/j.cardiores.2006.04.010;
RA   Tu C.-F., Su Y.-H., Huang Y.-N., Tsai M.-T., Li L.-T., Chen Y.-L.,
RA   Cheng C.-J., Dai D.-F., Yang R.-B.;
RT   "Localization and characterization of a novel secreted protein SCUBE1
RT   in human platelets.";
RL   Cardiovasc. Res. 71:486-495(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
CC   -!- FUNCTION: Could function as an adhesive molecule and its matrix
CC       bound and soluble fragments may play a critical role in vascular
CC       biology. {ECO:0000269|PubMed:16753137}.
CC   -!- SUBUNIT: Forms homooligomers and heterooligomers with SCUBE2 and
CC       SCUBE3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12270931,
CC       ECO:0000269|PubMed:16753137}. Cell membrane
CC       {ECO:0000269|PubMed:16753137}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16753137}.
CC   -!- TISSUE SPECIFICITY: Detected in endothelial cells. Highly
CC       expressed in platelets. Stored in platelet alpha granules, and
CC       transferred to the cell surface upon activation and aggregation. A
CC       smaller form, probably produced by limited proteolysis, after
CC       being released from the storage granules, is associated with
CC       thrombus and localized with the subendothelial matrices in
CC       atherosclerotic plaques. {ECO:0000269|PubMed:12270931,
CC       ECO:0000269|PubMed:16753137}.
CC   -!- INDUCTION: Down-regulated by inflammatory cytokines.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12270931}.
CC   -!- PTM: Could be proteolytically cleaved to release a smaller active
CC       fragment.
DR   EMBL; AF525689; AAN77133.1; -; mRNA.
DR   EMBL; Z99756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z82214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS14048.1; -.
DR   RefSeq; NP_766638.2; NM_173050.3.
DR   UniGene; Hs.133995; -.
DR   ProteinModelPortal; Q8IWY4; -.
DR   SMR; Q8IWY4; -.
DR   STRING; 9606.ENSP00000354080; -.
DR   iPTMnet; Q8IWY4; -.
DR   PhosphoSitePlus; Q8IWY4; -.
DR   BioMuta; SCUBE1; -.
DR   DMDM; 145559527; -.
DR   jPOST; Q8IWY4; -.
DR   PaxDb; Q8IWY4; -.
DR   PeptideAtlas; Q8IWY4; -.
DR   PRIDE; Q8IWY4; -.
DR   ProteomicsDB; 70926; -.
DR   DNASU; 80274; -.
DR   Ensembl; ENST00000360835; ENSP00000354080; ENSG00000159307.
DR   GeneID; 80274; -.
DR   KEGG; hsa:80274; -.
DR   UCSC; uc003bdt.3; human.
DR   CTD; 80274; -.
DR   DisGeNET; 80274; -.
DR   EuPathDB; HostDB:ENSG00000159307.18; -.
DR   GeneCards; SCUBE1; -.
DR   H-InvDB; HIX0027842; -.
DR   HGNC; HGNC:13441; SCUBE1.
DR   HPA; HPA003190; -.
DR   MIM; 611746; gene.
DR   neXtProt; NX_Q8IWY4; -.
DR   OpenTargets; ENSG00000159307; -.
DR   PharmGKB; PA35019; -.
DR   eggNOG; ENOG410IR7D; Eukaryota.
DR   eggNOG; ENOG411030G; LUCA.
DR   GeneTree; ENSGT00940000153185; -.
DR   HOGENOM; HOG000230943; -.
DR   HOVERGEN; HBG054902; -.
DR   InParanoid; Q8IWY4; -.
DR   OMA; SINKQQF; -.
DR   OrthoDB; 73164at2759; -.
DR   PhylomeDB; Q8IWY4; -.
DR   TreeFam; TF351672; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   GenomeRNAi; 80274; -.
DR   PRO; PR:Q8IWY4; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000159307; Expressed in 172 organ(s), highest expression level in islet of Langerhans.
DR   ExpressionAtlas; Q8IWY4; baseline and differential.
DR   Genevisible; Q8IWY4; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0007512; P:adult heart development; NAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; NAS:UniProtKB.
DR   GO; GO:0045446; P:endothelial cell differentiation; NAS:UniProtKB.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; NAS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR   CDD; cd00041; CUB; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF07699; Ephrin_rec_like; 3.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF57184; SSF57184; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 6.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 6.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    988       Signal peptide, CUB and EGF-like domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000254648.
FT   DOMAIN       33     73       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN       74    116       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      117    153       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      166    202       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      206    241       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      245    280       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      282    322       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      323    361       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      362    402       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      798    910       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   CARBOHYD    370    370       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    466    466       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    679    679       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    750    750       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    779    779       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    789    789       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     37     50       {ECO:0000250}.
FT   DISULFID     44     59       {ECO:0000250}.
FT   DISULFID     61     72       {ECO:0000250}.
FT   DISULFID     78     91       {ECO:0000250}.
FT   DISULFID     87    100       {ECO:0000250}.
FT   DISULFID    102    115       {ECO:0000250}.
FT   DISULFID    121    132       {ECO:0000250}.
FT   DISULFID    128    141       {ECO:0000250}.
FT   DISULFID    286    297       {ECO:0000250}.
FT   DISULFID    293    306       {ECO:0000250}.
FT   DISULFID    308    321       {ECO:0000250}.
FT   DISULFID    327    337       {ECO:0000250}.
FT   DISULFID    333    346       {ECO:0000250}.
FT   DISULFID    348    360       {ECO:0000250}.
FT   DISULFID    366    377       {ECO:0000250}.
FT   DISULFID    373    386       {ECO:0000250}.
FT   DISULFID    388    401       {ECO:0000250}.
FT   DISULFID    798    824       {ECO:0000250}.
FT   DISULFID    851    872       {ECO:0000250}.
FT   VARIANT     398    398       G -> R (in dbSNP:rs129415).
FT                                {ECO:0000269|PubMed:12270931}.
FT                                /FTId=VAR_028850.
FT   VARIANT     648    648       S -> P (in dbSNP:rs138993).
FT                                {ECO:0000269|PubMed:12270931}.
FT                                /FTId=VAR_028851.
FT   CONFLICT     53     53       T -> A (in Ref. 1; AAN77133).
FT                                {ECO:0000305}.
FT   CONFLICT     73     73       E -> G (in Ref. 1; AAN77133).
FT                                {ECO:0000305}.
FT   CONFLICT    234    234       L -> P (in Ref. 1; AAN77133).
FT                                {ECO:0000305}.
SQ   SEQUENCE   988 AA;  107910 MW;  AB2C2AB53F3D3C2B CRC64;
     MGAAAVRWHL CVLLALGTRG RLAGGSGLPG SVDVDECSEG TDDCHIDAIC QNTPKSYKCL
     CKPGYKGEGK QCEDIDECEN DYYNGGCVHE CINIPGNYRC TCFDGFMLAH DGHNCLDVDE
     CQDNNGGCQQ ICVNAMGSYE CQCHSGFFLS DNQHTCIHRS NEGMNCMNKD HGCAHICRET
     PKGGVACDCR PGFDLAQNQK DCTLTCNYGN GGCQHSCEDT DTGPTCGCHQ KYALHSDGRT
     CIETCAVNNG GCDRTCKDTA TGVRCSCPVG FTLQPDGKTC KDINECLVNN GGCDHFCRNT
     VGSFECGCRK GYKLLTDERT CQDIDECSFE RTCDHICINS PGSFQCLCHR GYILYGTTHC
     GDVDECSMSN GSCDQGCVNT KGSYECVCPP GRRLHWNGKD CVETGKCLSR AKTSPRAQLS
     CSKAGGVESC FLSCPAHTLF VPDSENSYVL SCGVPGPQGK ALQKRNGTSS GLGPSCSDAP
     TTPIKQKARF KIRDAKCHLR PHSQARAKET ARQPLLDHCH VTFVTLKCDS SKKRRRGRKS
     PSKEVSHITA EFEIETKMEE ASDTCEADCL RKRAEQSLQA AIKTLRKSIG RQQFYVQVSG
     TEYEVAQRPA KALEGQGACG AGQVLQDSKC VACGPGTHFG GELGQCVSCM PGTYQDMEGQ
     LSCTPCPSSD GLGLPGARNV SECGGQCSPG FFSADGFKPC QACPVGTYQP EPGRTGCFPC
     GGGLLTKHEG TTSFQDCEAK VHCSPGHHYN TTTHRCIRCP VGTYQPEFGQ NHCITCPGNT
     STDFDGSTNV THCKNQHCGG ELGDYTGYIE SPNYPGDYPA NAECVWHIAP PPKRRILIVV
     PEIFLPIEDE CGDVLVMRKS ASPTSITTYE TCQTYERPIA FTSRSRKLWI QFKSNEGNSG
     KGFQVPYVTY DEDYQQLIED IVRDGRLYAS ENHQEILKDK KLIKALFDVL AHPQNYFKYT
     AQESKEMFPR SFIKLLRSKV SRFLRPYK
//
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