NCA11_XENLA
ID NCA11_XENLA Reviewed; 1088 AA.
AC P16170;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Neural cell adhesion molecule 1-A;
DE Short=N-CAM-1-A;
DE Short=NCAM-1-A;
DE Flags: Precursor;
GN Name=ncam1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=2481269; DOI=10.1093/nar/17.24.10321;
RA Krieg P.A., Sakaguchi D.S., Kintner C.R.;
RT "Primary structure and developmental expression of a large cytoplasmic
RT domain form of Xenopus laevis neural cell adhesion molecule (NCAM).";
RL Nucleic Acids Res. 17:10321-10335(1989).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=N-CAM 180;
CC IsoId=P16170-1; Sequence=Displayed;
CC Name=2; Synonyms=N-CAM 140;
CC IsoId=P16170-2; Sequence=VSP_002589;
CC -!- TISSUE SPECIFICITY: Expressed in neuron and in presumptive neural
CC tissue.
CC -!- DEVELOPMENTAL STAGE: The mRNA encoding this LD-NCAM is the major
CC transcript present in both maternal RNA and in the embryo during early
CC neural development.
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DR EMBL; M25696; AAA49909.1; -; mRNA.
DR PIR; S09600; IJXLNL.
DR RefSeq; NP_001081296.1; NM_001087827.1. [P16170-1]
DR AlphaFoldDB; P16170; -.
DR SMR; P16170; -.
DR DNASU; 397761; -.
DR GeneID; 397761; -.
DR KEGG; xla:397761; -.
DR CTD; 397761; -.
DR Xenbase; XB-GENE-6252598; ncam1.S.
DR OrthoDB; 129648at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 397761; Expressed in heart and 16 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 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; IPR033019; Ncam1.
DR InterPro; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231:SF239; PTHR12231:SF239; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 2.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT CHAIN 20..1088
FT /note="Neural cell adhesion molecule 1-A"
FT /id="PRO_0000015016"
FT TOPO_DOM 20..705
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..108
FT /note="Ig-like C2-type 1"
FT DOMAIN 113..202
FT /note="Ig-like C2-type 2"
FT DOMAIN 209..294
FT /note="Ig-like C2-type 3"
FT DOMAIN 303..397
FT /note="Ig-like C2-type 4"
FT DOMAIN 400..484
FT /note="Ig-like C2-type 5"
FT DOMAIN 493..592
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 594..690
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 758..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..153
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT BINDING 158..162
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..93
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT DISULFID 136..186
FT /evidence="ECO:0000250|UniProtKB:P13595"
FT DISULFID 232..282
FT /evidence="ECO:0000250|UniProtKB:P13590"
FT DISULFID 323..379
FT /evidence="ECO:0000305"
FT DISULFID 420..473
FT /evidence="ECO:0000305"
FT VAR_SEQ 804..1049
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2481269"
FT /id="VSP_002589"
SQ SEQUENCE 1088 AA; 117778 MW; 62738B55B03F3E83 CRC64;
MLHIKDLIWT LYFIGTAVAL EVNIVPDQGE ISLGESKFFL CQVSGEATDI SWYSPTGEKL
VTQQQISVVR SDDYTSTLTI YNASSQDAGI YKCVASNEAE GESEGTVNLK IYQKLTFKNA
PTPQEFKEGE DAVIICDVSS SIPSIITWRH KGKDVIFKKD VRFVVLANNY LQIRGIKKTD
EGTYRCEGRI LARGEINYKD IQVIVNVPPT IQARQLRVNA TANMAESVVL SCDADGFPDP
EISWLKKGEP IEDGEEKISF NEDQSEMTIH HVEKDDEAEY SCIANNQAGE AEATILLKVY
AKPKITYVEN KTAVELDEIT LTCEASGDPI PSITWRTAVR NISSEATTLD GHIVVKEHIR
MSALTLKDIQ YTDAGEYFCI ASNPIGVDMQ AMYFEVQYAP KIRGPVVVYT WEGNPVNITC
EVFAHPRAAV TWFRDGQLLP SSNFSNIKIY SGPTSSSLEV NPDSENDFGN YNCTAINTIG
HEFSEFILVQ ADTPSSPAIR KVEPYSSTVM IVFDEPDSTG GVPILKYKAE WRVIGHEKWH
TKYYDAKEVN AESIITVMGL KPETSYMVKL SAMNGKGLGD STPSQEFTTQ PVREPSAPKL
VGHLSEDGNS IKVDILKQDD GGSPIRHYLV NYRALNALEW KPEMRVPSNS HHVMLKALEW
NVDYEVIVVA ENQQGKSKPA LLSFRTTAKP TATTATASAG TGLGTGAIVG ILIVIFVLLL
VVVDVTCFFL NKCGLLMCIA VNFCGKAGPG AKGKDIEEGK AAFSKDESKE PIVEVRTEEE
RTPNHDGSNQ IEPNETTPLT EPEHPAAVED MLPSVTTVTT NSDTITETFA TAQNSPTSET
TTLTSSTAPP PTTAPDSNTI QSIQATPSKA EAPTTSSPPP TSSPKVAPLV DLSDTPTNNP
SKVVANQAGP LNPSAATSAA EPPTVIIKPV TTVPPNAASP PPTPEPKQVK QEQSGTKSPE
KEEAQPSTVK NPTEATKDES ASLSNTKPLQ DEDFQIDGGT FKTPEIDLAK DVFAALGTAT
PTAVASGKAS ELVSSTADTS VPLDSAKTEK TQVEEKSKPE EIDVKGTPAE VKTVPNEATQ
TNANESKA
