CDCP1_MOUSE
ID CDCP1_MOUSE Reviewed; 833 AA.
AC Q5U462; Q810J0; Q921M9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=CUB domain-containing protein 1;
DE AltName: Full=Membrane glycoprotein gp140;
DE AltName: Full=Transmembrane and associated with src kinases;
DE AltName: CD_antigen=CD318;
DE Flags: Precursor;
GN Name=Cdcp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Pancreas;
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).
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.
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 SRC and PRKCG/protein kinase C gamma (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=Its shedding may lead to a soluble peptide.
CC {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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 the N-terminal side. Converted to p80 by plasmin,
CC a trypsin-like protease (By similarity). {ECO:0000250}.
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DR EMBL; BC011340; AAH11340.1; -; mRNA.
DR EMBL; BC050137; AAH50137.1; -; mRNA.
DR EMBL; BC085253; AAH85253.1; -; mRNA.
DR CCDS; CCDS23657.1; -.
DR RefSeq; NP_598735.2; NM_133974.3.
DR AlphaFoldDB; Q5U462; -.
DR IntAct; Q5U462; 1.
DR STRING; 10090.ENSMUSP00000042057; -.
DR GlyGen; Q5U462; 7 sites.
DR iPTMnet; Q5U462; -.
DR PhosphoSitePlus; Q5U462; -.
DR MaxQB; Q5U462; -.
DR PaxDb; Q5U462; -.
DR PeptideAtlas; Q5U462; -.
DR PRIDE; Q5U462; -.
DR ProteomicsDB; 281280; -.
DR Antibodypedia; 2564; 843 antibodies from 44 providers.
DR DNASU; 109332; -.
DR Ensembl; ENSMUST00000039229; ENSMUSP00000042057; ENSMUSG00000035498.
DR GeneID; 109332; -.
DR KEGG; mmu:109332; -.
DR UCSC; uc009sfz.1; mouse.
DR CTD; 64866; -.
DR MGI; MGI:2442010; Cdcp1.
DR VEuPathDB; HostDB:ENSMUSG00000035498; -.
DR eggNOG; ENOG502QVKN; Eukaryota.
DR GeneTree; ENSGT00390000010209; -.
DR HOGENOM; CLU_007498_0_0_1; -.
DR InParanoid; Q5U462; -.
DR OMA; RFVPGCF; -.
DR OrthoDB; 223122at2759; -.
DR PhylomeDB; Q5U462; -.
DR TreeFam; TF331392; -.
DR BioGRID-ORCS; 109332; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q5U462; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5U462; protein.
DR Bgee; ENSMUSG00000035498; Expressed in paneth cell and 139 other tissues.
DR Genevisible; Q5U462; MM.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..833
FT /note="CUB domain-containing protein 1"
FT /id="PRO_0000226250"
FT TOPO_DOM 30..666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 417..540
FT /note="CUB"
FT REGION 783..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 368..369
FT /note="Cleavage; by ST14/MT-SP1"
FT /evidence="ECO:0000250"
FT MOD_RES 731
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5V8"
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 342
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"
SQ SEQUENCE 833 AA; 92726 MW; 1F1423DD595C6B27 CRC64;
MAHSACGFSV ALLGALLLGT ARLLRGTEAS EIALPQRSGV TVSIKLGNPA LPVKICYIVM
SRQHITELII RPGERKSFTF SCSNPEKHFV LKIEKNIDCM SGPCPFGEVH LQPSTSELPI
LNRTFIWDVR AHKSIGLELQ FATPRLRQIG PGESCADGVT HSISGHIDAT EVRIGTFCSN
GTVSRIKMQE GVKMALHLPW FHRRNVSGFS IANRSSIKRL CIIESVFEGE GSATLMSANY
PGGFPEDELM TWQFVVPAHL RASVSFLNFN VSNCERKEER VEYYIPGSTT NPEVFRLEDK
QPGNMAGNFN LSLQGCDQDA QSPGILRLQF QVLVQRPQDE SNKTYMVDLS RERTMSLTIE
PRPVKHGRRF VPGCFVCLES RTCSTNVTLT AGSIHKISFL CDDLTRLWVN VEKTLSCLDH
RYCYRQSFKL QVPDYILQLP VQLHDFSWKL LVPKDKLSLM LVPGQKLQQH TQERPCNTSF
GYHVTSTTPG QDLYFGSFCS GGSIEKIQVK QNSSVTLRAY APSFQQEVSK QGLIVSYTPY
FKEEGIFTVT PDTKNKVYLR SPNWDRGLPA LSSVSWNISV PSNQVACLTV LKERSGLACQ
SGRAFMIIQE QQSRAEEIFS LEEEVLPKPS FHHHSFWVNI SNCSPMNGKQ LDLLFWVTLT
PRTVDLAVVI GAAGGGALLL FALVLIICFV KKKKKVDKGP AVGIYNGNVN TQMPQTQKFP
KGRKDNDSHV YAVIEDTMVY GHLLQDSGGS FIQPEVDTYR PFQGPMGDCP PTPPPLFSRT
PTAKFTAEEL APSSPPESES EPYTFSHPNK GEIGVRETDI PLLHTQGPVE TEE
