ID A0A2K5M4A5_CERAT Unreviewed; 846 AA.
AC A0A2K5M4A5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Neural cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSCATP00000020018.1};
GN Name=NCAM1 {ECO:0000313|Ensembl:ENSCATP00000020018.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000020018.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000020018.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC {ECO:0000256|ARBA:ARBA00003000}.
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DR AlphaFoldDB; A0A2K5M4A5; -.
DR Ensembl; ENSCATT00000044203.1; ENSCATP00000020018.1; ENSCATG00000032945.1.
DR GeneTree; ENSGT00940000155743; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000032945; Expressed in frontal cortex and 8 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05865; IgI_1_NCAM-1; 1.
DR CDD; cd05869; IgI_NCAM-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1.
DR PANTHER; PTHR12231:SF239; NEURAL CELL ADHESION MOLECULE 1; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 3.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 4: Predicted;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..846
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014328385"
FT TRANSMEM 711..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..110
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 115..188
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 211..300
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 307..402
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 405..490
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 498..597
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 599..694
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 754..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 93282 MW; FCF21365AFAA8F85 CRC64;
MFELDFVFVL FCFVFSASLQ VDIVPSQGEI SVGESKFFLC QVAGDAKDKD ISWFSPNGEK
LTPNQQRISV VWNDDSSSTL TIYNANIDDA GIYKCVVTGE DGSESEATVN VKIFQKLMFK
NAPTPQEFRE GEDAVIVCDV VSSLPPTIIW KHKGRDVILK KDVRFIVLSN NYLQIRGIKK
TDEGTYRCEG RILARGEINF KDIQVVVNVP PTIQARQNIV NATANLGQSV TLVCDAEGFP
EPTMSWTKDG EQIEQEEDDE KYIFSDDSSQ LTIKKVDKND EAEYICIAEN KAGEQDATIH
LKVFAKPKIT YVENQTAMEL EEQVTLTCEA SGDPIPSITW RTSTRNISSE EKTLDGHMVV
RSHARVSSLT LKSIQYTDAG EYICTASNTI GQDSQSMYLE VQYAPKLQGP VAVYTWEGNQ
VNITCEVFAY PSATISWFRD GQLLPSSNYS NIKIYNTPSA SYLEVTPDSE NDFGNYNCTA
VNRIGQESLE FILVQADTPS SPSIDQVEPY SSTAQVQFDE PEATGGVPIL KYKAEWRAVG
EEVWHSKWYD AKEASMEGIV TIVGLKPETT YAVRLAALNG KGLGEISAAS EFKTQPVREP
SAPKLEGQMG EDGNSIKVNL IKQDDGGSPI RHYLVRYRAL SSEWKPEIRL PSGSDHVMLK
SLDWNAEYEV YVVAENQQGK SKAAHFVFRT SAQPTAIPAN GSPTSGLSTG AIVGILIVIF
VLLLVVVDIT CYFLNKCGLF MCIAVNLCGK AGPGAKGKDM EEGKAAFSKD ESKEPIVEVR
TEEERTPNHD GGKHTEPNET TPLTEPEKGP VEAKPECQET ETKPAPAEVK TVPNDATQTK
ENESKA
//
