ID A0A2R8MRU7_CALJA Unreviewed; 1114 AA.
AC A0A2R8MRU7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Neural cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSCJAP00000064075.3};
GN Name=NCAM1 {ECO:0000313|Ensembl:ENSCJAP00000064075.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000064075.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000064075.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000064075.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A2R8MRU7; -.
DR Ensembl; ENSCJAT00000084091.3; ENSCJAP00000064075.3; ENSCJAG00000012342.5.
DR GeneTree; ENSGT00940000155743; -.
DR Proteomes; UP000008225; Chromosome 11.
DR Bgee; ENSCJAG00000012342; Expressed in cerebellum and 6 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:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 707..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..96
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 101..174
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 197..286
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 293..398
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 401..486
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 494..593
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 595..690
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 750..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 119202 MW; F5F705678E79014C CRC64;
MDFSLQVDIV PSQGEISVGE SKFFLCQVAG DAKDKDISWF SPNGEKLTPN QQRISVVWND
DSSSTLTIYN ANIDDAGIYK CVVTDEEGSE SEATVNVKIF QKLMFKNAPT PQEFREGEDA
VIICDVVSSL PPTIIWKHKG RDVILKKDVR FIVLSNNYLQ IRGIKKTDEG TYRCEGRILA
RGEINFKDIQ VIVNVPPTIQ ARQNIVNATA NLGQSVTLVC DAEGFPEPTM SWTKDGEQIE
QEEDNEKYIF SDDSSQLTIR KVDKNDEAEY VCIAENKAGE QDATIHLKVF AKPKITYVEN
QTAMELEEQV TLTCEASGDP IPSITWRTST RNISSEEKAS WTRPEKQETL DGHMVVRSHA
RVSSLTLKSI QYTDAGEYIC TASNTIGQDS QSMYLEVQYA PKLQGPVAVY TWEGNQVNIT
CEVFAYPSAT ISWFRDGQLL PSSNYSNIKI YNTPSASYLE VTPDSENDFG NYNCTAVNRI
GQESLEFILV QADTPSSPSI DQVEPYSSTA QVQFDEPEAT GGVPILKYKA EWRAMGEEVW
HSKWYDAKEA SMEGIVTIVG LKPETTYAVR LAALNGKGLG EISAASEFKT QPVREPSAPK
LEGQMGEDGN SIKVNLIKQD DGGSPIRHYL VKYRALSSEW KPEIRLPSGS DHVMLKSLEW
NAEYEVYVVA ENQQGKSKAA HFVFRTSAQP TAIPANGSPT SGLSTGAIVG ILIVIFVLLL
VVVDITCYFL NKCGLFMCIA VNLCGKAGPG AKGKDMEEGK AAFSKDESKE PIVEVRTEEE
RTPNHDGGKH TEPNETTPLT EPELPADTTA TVEDMLPSVT TVTTNSDTIT ETFATAQNSP
TSETTTLTSS IAPPATATPD SNSVPAGQAT PSKGPSASTS SPAPAAAPKV APLVDLSDTP
TSTPATSNLS SSVLANQGAV LSPSAPASVG EASKAPPASK PSPAPVPTPT GAASSLAAAA
APATEAPQAK QESPSTKGPD PEPTQPGAVK SPPEAATALA SPKSEAASVS TTNPSQGEDF
KMDEGNFKTP DIDLAKDVFA ALGSPAPAAG ASGQAPELAP STADSSVSPA PAKTEKGPVE
AKPECQETET KPAPAEVKTV PNDATQTKEN ESKA
//
