ID G3SZJ2_LOXAF Unreviewed; 644 AA.
AC G3SZJ2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Melanoma cell adhesion molecule {ECO:0000313|Ensembl:ENSLAFP00000006039.3};
GN Name=MCAM {ECO:0000313|Ensembl:ENSLAFP00000006039.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000006039.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000006039.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006039.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000006039.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006039.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_003418238.1; XM_003418190.2.
DR AlphaFoldDB; G3SZJ2; -.
DR STRING; 9785.ENSLAFP00000006039; -.
DR Ensembl; ENSLAFT00000007176.3; ENSLAFP00000006039.3; ENSLAFG00000007173.3.
DR GeneID; 100659183; -.
DR KEGG; lav:100659183; -.
DR CTD; 4162; -.
DR eggNOG; ENOG502QV1U; Eukaryota.
DR GeneTree; ENSGT00940000155838; -.
DR HOGENOM; CLU_028888_3_0_1; -.
DR InParanoid; G3SZJ2; -.
DR OMA; DARFYCE; -.
DR OrthoDB; 5313595at2759; -.
DR TreeFam; TF330534; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0061042; P:vascular wound healing; IEA:Ensembl.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11973:SF18; CELL SURFACE GLYCOPROTEIN MUC18; 1.
DR PANTHER; PTHR11973; CELL SURFACE GLYCOPROTEIN MUC18-RELATED; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..644
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003454399"
FT TRANSMEM 558..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 138..241
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 243..329
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 342..422
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 429..515
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 523..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71012 MW; 6538CE881515CCE9 CRC64;
MELPELVCVF LLAACCHCRR AVGVPGEAEQ PAPEVLEVEV GSTALLKCGP ARSQDSLSLD
WFSVHKEKPT LIYRVRQGQG QSEPGEYQHR LSLQDKGATL ALAHVTPHDE RIFLCQGKRP
RSQEHRIQLQ VYKAPEEPSI QVNTLGISVN SEEPEEVATC VGRNGYPVPQ VTWYKNRLPL
KEEKNRVHIQ SSQIVESSGL YTLQSILKAR LVKEDKDAQF YCELSYRLPS GNHMKESREV
TVPVFYPAEK LWVEVVPTGM LKEGDHVEIR CLADGNPPPH FIISKQNPST MEMEEKATDH
DGLLVLEPAR KEHSGLYECQ GLDLDTTVSL MDQQELLVNY VSDVRVSPTT PESHEGSSLT
LTCEAESNQA LEFLWLREKT GKVLEKGPVL LLHNLKREAA GGYLCMASVP SVPGLNSTQL
VNVAIYGSPW MASKERKLWV KENEVMRLSC EASGHPRPTI SWSVNGTAHE QDKDPQSVLS
TLNVLVTPDL LETGAECVAS NPLGRNSTVI RLELVNLTTL PPDSTATTGL STSTASPHAR
ANSTSAEKKL PEPESKGVVI VAVIVCILVL AVLGAVLYFF YKKGKLPCGR SGKQEITLPP
LRKSEIVVEV KSDKLPEEMG LLQGSNGDKR APGDQGEKYI DLRH
//
