HECAM_MOUSE
ID HECAM_MOUSE Reviewed; 418 AA.
AC Q640R3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Hepatocyte cell adhesion molecule;
DE Short=Protein hepaCAM;
DE Flags: Precursor;
GN Name=Hepacam {ECO:0000312|MGI:MGI:1920177};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH82537.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-418.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH82537.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH82537.1};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-321; SER-352 AND
RP SER-379, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in regulating cell motility and cell-matrix
CC interactions. May inhibit cell growth through suppression of cell
CC proliferation (By similarity). {ECO:0000250|UniProtKB:Q14CZ8}.
CC -!- SUBUNIT: Homodimer. Dimer formation occurs predominantly through cis
CC interactions on the cell surface (By similarity). Part of a complex
CC containing MLC1, TRPV4, AQP4 and ATP1B1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Single-pass
CC type I membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q14CZ8}. Note=Colocalizes with CDH1.
CC {ECO:0000250|UniProtKB:Q14CZ8}.
CC -!- DOMAIN: The cytoplasmic domain plays an important role in regulation of
CC cell-matrix adhesion and cell motility. {ECO:0000250|UniProtKB:Q14CZ8}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q14CZ8}.
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DR EMBL; AC138284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082537; AAH82537.1; -; mRNA.
DR CCDS; CCDS22976.1; -.
DR RefSeq; NP_780398.2; NM_175189.4.
DR AlphaFoldDB; Q640R3; -.
DR SMR; Q640R3; -.
DR BioGRID; 215649; 2.
DR STRING; 10090.ENSMUSP00000054105; -.
DR GlyConnect; 2372; 19 N-Linked glycans (2 sites).
DR GlyGen; Q640R3; 4 sites, 19 N-linked glycans (2 sites).
DR iPTMnet; Q640R3; -.
DR PhosphoSitePlus; Q640R3; -.
DR SwissPalm; Q640R3; -.
DR MaxQB; Q640R3; -.
DR PaxDb; Q640R3; -.
DR PRIDE; Q640R3; -.
DR ProteomicsDB; 270898; -.
DR Antibodypedia; 2574; 200 antibodies from 30 providers.
DR DNASU; 72927; -.
DR Ensembl; ENSMUST00000051839; ENSMUSP00000054105; ENSMUSG00000046240.
DR GeneID; 72927; -.
DR KEGG; mmu:72927; -.
DR UCSC; uc009our.1; mouse.
DR CTD; 220296; -.
DR MGI; MGI:1920177; Hepacam.
DR VEuPathDB; HostDB:ENSMUSG00000046240; -.
DR eggNOG; ENOG502QPJB; Eukaryota.
DR GeneTree; ENSGT01010000222242; -.
DR HOGENOM; CLU_058570_1_0_1; -.
DR InParanoid; Q640R3; -.
DR OMA; DRKNPMA; -.
DR OrthoDB; 905929at2759; -.
DR PhylomeDB; Q640R3; -.
DR TreeFam; TF331199; -.
DR BioGRID-ORCS; 72927; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Hepacam; mouse.
DR PRO; PR:Q640R3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q640R3; protein.
DR Bgee; ENSMUSG00000046240; Expressed in lumbar subsegment of spinal cord and 86 other tissues.
DR ExpressionAtlas; Q640R3; baseline and differential.
DR Genevisible; Q640R3; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell cycle; Cytoplasm; Disulfide bond; Glycoprotein;
KW Growth arrest; Growth regulation; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..418
FT /note="Hepatocyte cell adhesion molecule"
FT /evidence="ECO:0000255"
FT /id="PRO_0000298778"
FT TOPO_DOM 34..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..142
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT DOMAIN 148..234
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 271..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 168..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 418 AA; 46367 MW; 39D65EB953A5B933 CRC64;
MKRERGALSR ASRALRLSPF VYLLLIQPVP LEGVNITSPV RLIHGTVGKS ALLSVQYSST
SSDKPVVKWQ LKRDKPVTVV QSIGTEVIGT LRPDYRDRIR LFENGSLLLS DLQLADEGTY
EVEISITDDT FTGEKTINLT VDVPISRPQV LVASTTVLEL SEAFTLNCSH ENGTKPSYTW
LKDGKPLLND SRMLLSPDQK VLTITRVLME DDDLYSCVVE NPISQVRSLP VKITVYRRSS
LYIILSTGGI FLLVTLVTVC ACWKPSKKSR KKRKLEKQNS LEYMDQNDDR LKSEADTLPR
SGEQERKNPM ALYILKDKDS SEPDENPATE PRSTTEPGPP GYSVSPPVPG RSPGLPIRSA
RRYPRSPARS PATGRTHTSP PRAPSSPGRS RSSSRSLRTA GVQRIREQDE SGQVEISA
