HECAM_BOVIN
ID HECAM_BOVIN Reviewed; 418 AA.
AC A4FUY1; Q58DG9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Hepatocyte cell adhesion molecule;
DE Short=Protein hepaCAM;
DE Flags: Precursor;
GN Name=HEPACAM {ECO:0000250|UniProtKB:Q14CZ8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI23428.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI23428.1};
RC TISSUE=Thalamus {ECO:0000312|EMBL:AAI23428.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A4FUY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4FUY1-2; Sequence=VSP_052495, VSP_052496;
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; BT021628; AAX46475.1; -; mRNA.
DR EMBL; BC123427; AAI23428.1; -; mRNA.
DR RefSeq; NP_001026929.2; NM_001031759.2. [A4FUY1-1]
DR AlphaFoldDB; A4FUY1; -.
DR SMR; A4FUY1; -.
DR PaxDb; A4FUY1; -.
DR GeneID; 521015; -.
DR KEGG; bta:521015; -.
DR CTD; 220296; -.
DR eggNOG; ENOG502QPJB; Eukaryota.
DR HOGENOM; CLU_058570_1_0_1; -.
DR InParanoid; A4FUY1; -.
DR OrthoDB; 905929at2759; -.
DR TreeFam; TF331199; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell cycle; Cytoplasm; Disulfide bond;
KW Glycoprotein; Growth arrest; Growth regulation; Immunoglobulin domain;
KW Membrane; 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_0000298776"
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..141
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..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640R3"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640R3"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640R3"
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"
FT VAR_SEQ 238..249
FT /note="RSSLYIILSTGG -> ESPATLPWDSQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_052495"
FT VAR_SEQ 250..418
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_052496"
SQ SEQUENCE 418 AA; 46057 MW; 467D2A83419E518F CRC64;
MKREREAPSR AFSALRLAPF VYLLLIQTEP LEGVNITSPV RLIHGTVGKA ALLSVQYSST
SSDKPVVKWQ LKRDKPVTVV QSIGTEVIGT LRPDYRDRIR LFENGSLLLS DLQLADEGTY
EVEISITDDT FTGEKTINLT VDVPISRPQV LVASTTVLEL SEAFTLNCSH ENGTKPSYTW
LKDGKPLLND SRMLLSPDQK VLTITRVLME DDDLYSCVVE NPISQGRSPP VKITVYRRSS
LYIILSTGGI FLLVTLVTVC ACWKPSKKSG KKRKLEKQNS MEYMDQSDDR LKPEADTLPR
SGEQERKNPM ALYILKDKDS PEPEENPASE PRSAAEPGPP GYSVSPAVPG RSPGLPIRSA
RRYPRSPARS PATGRTHSSP PRAPGSPGRS RSASRTLRTA GVHLIREQDE AGPVEISA
