ID A0A2K5KH26_COLAP Unreviewed; 858 AA.
AC A0A2K5KH26;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Neural cell adhesion molecule 1 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000040390.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000040390.1}
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 RefSeq; XP_011782147.1; XM_011926757.1.
DR AlphaFoldDB; A0A2K5KH26; -.
DR Ensembl; ENSCANT00000063655.1; ENSCANP00000040390.1; ENSCANG00000043881.1.
DR GeneID; 105501034; -.
DR CTD; 4684; -.
DR OMA; DSKQKGQ; -.
DR OrthoDB; 5233206at2759; -.
DR Proteomes; UP000233080; Unplaced.
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:UP000233080};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..858
FT /note="Neural cell adhesion molecule 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014404082"
FT TRANSMEM 723..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..111
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 116..189
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 212..301
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 308..413
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 416..501
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 509..608
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 611..706
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 766..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 94531 MW; 46E83B46CEA8DFCB CRC64;
MLQTKNLIWT LFFLGTAASL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
KLTPNQQRIS VVWNDDSSST LTIYNANIDD AGIYKCVVTG EDGSESEATV NVKIFQKLMF
KNAPTPQEFR EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVVVNV PPTIQARQNI VNATANLGQS VTLVCDAEGF
PEPTMSWTKD GEQIEQEEDD EKYIFSDDSS QLTIKKVDKN DEAEYICIAE NKAGEQDATI
HLKVFAKPKI TYVENQTAME LEEQVTLTCE ASGDPIPSIT WRTSTRNISS EEKASWTRPE
KQETLDGHMV VRSHARVSSL TLKSIQYTDA GEYICTASNT IGQDSQSMYL EVQYAPKLQG
PVAVYTWEGN QVNITCEVFA YPSATISWFR DGQLLPSSNY SNIKIYNTPS ASYLEVTPDS
ENDFGNYNCT AVNRIGQESL EFILVQADTP SSPSIDQVEP YSSTAQVQFD EPEATGGVPI
LKYKAEWRAV GEEVWHSKWY DAKEASMEGI VTIVGLKPET TYAVRLAALN GKGLGEISAA
SEFKTQPVQG EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVRYR ALSSEWKPEI
RLPSGSDHVM LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTSGLS
TGAIVGILIV IFVLLLVVVD ITCYFLNKCG LFMCIAVNLC GKAGPGAKGK DMEEGKAAFS
KDESKEPIVE VRTEEERTPN HDGGKHTEPN ETTPLTEPEK GPVEAKPECQ ETETKPAPAE
VKTVPNDATQ TKENESKA
//
