NCA12_XENLA
ID NCA12_XENLA Reviewed; 1092 AA.
AC P36335;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Neural cell adhesion molecule 1-B;
DE Short=N-CAM-1-B;
DE Short=NCAM-1-B;
DE Flags: Precursor;
GN Name=ncam1-b;
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].
RX PubMed=7684721; DOI=10.1016/0378-1119(93)90727-k;
RA Tonissen K.F., Krieg P.A.;
RT "Two neural-cell adhesion molecule (NCAM)-encoding genes in Xenopus laevis
RT are expressed during development and in adult tissues.";
RL Gene 127:243-247(1993).
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=1;
CC Comment=A number of isoforms are produced.;
CC Name=1; Synonyms=N-CAM 180;
CC IsoId=P36335-1; Sequence=Displayed;
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DR EMBL; M76710; AAA49910.1; -; mRNA.
DR PIR; JN0635; JN0635.
DR RefSeq; NP_001081298.1; NM_001087829.1. [P36335-1]
DR AlphaFoldDB; P36335; -.
DR SMR; P36335; -.
DR GeneID; 397762; -.
DR KEGG; xla:397762; -.
DR CTD; 397762; -.
DR Xenbase; XB-GENE-923178; ncam1.L.
DR OrthoDB; 129648at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 397762; Expressed in brain and 14 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; 3.
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 /evidence="ECO:0000250"
FT CHAIN 20..1092
FT /note="Neural cell adhesion molecule 1-B"
FT /id="PRO_0000015017"
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..1092
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 208..295
FT /note="Ig-like C2-type 3"
FT DOMAIN 303..397
FT /note="Ig-like C2-type 4"
FT DOMAIN 400..489
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 595..691
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 754..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1092
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"
SQ SEQUENCE 1092 AA; 118082 MW; CD236EE0EF8B7AD1 CRC64;
MLHIKDLIWT LYFIGAAVAL EVNIVPDQGE ISLGESKFFL CQVSGEATDI SWYSPTGEKL
LNQQQISVVK NDEYTSTLTI YNVSSQDAGI YKCVASSETE GESEGTVNLK IYQKLTFKYA
PTPQEFTEGE DAVIICDVSS SIPSIITWRH KGKDVIFKKD VRFVVLANNY LQIRGIKKTD
EGNYRCEGRI LARGEINYKD IQVIVNVPPL IQARQIRVNA TANMDESVVL SCDADGFPDP
EISWLKKGEP IEDGEEKISF NEDKSEMTIY RVEKEDEAEY SCIANNQAGE AEAIVLLKVY
AKPKMTYVEN KTTVELDEIT LTCEASGDPI PSITWRTAHR NISSEEKTLD GHIVVKDHIR
MSALTLKDIQ YTDAGEYFCV ASNPIGVDMQ AMYFEVQYAP KIRGPVVVYT WEGNPVNITC
DVLAHPSAAV SWFRDGQLLP SSNFSNIKIY NGPTFSSLEV NPDSENDFGN YNCSAVNSIG
HESSEFILVQ ADTPSSPAIR KVEPYSSTVM IVFDEPDATG GVPILKYKAE WRVVGQEKWH
ARYYDAKEVS AESIITVTGL KPETSYMVKL SAVNGKGLGD STPSQDFTTQ PVKGEPSAPK
LVGHLSEDGN SIKVDIIKQD DGGSPIRHYL VNYRALNAVD WKPEMRVPSN SHHVTLKTLE
WNVDYEVIVV AENQQGKSKQ ARLSFRTTAK PTATTATSAS TGLGTGAIVG ILIVTFVLLL
VVVDVTCFFL NKCGLLMCIA VNFCGKAGPG AKGKDIEEGK AAFSKDESKE PIVEVRTEEE
RTPNHDGSNQ IEPNETTPLT EPEHPADSTA TVEDMLPSVT TVTTNSDTIT ETFATAQNSP
TSETTTLTSS TAPPPSTAPD SNTVQSVQAT PSKAEVPTAS SPPPTSSPKV APLVDLSDTP
TNNPSKAVAN QAGALNPSAA TSAAEPPTAI IKPVTTVPAN TTSPPPTPEP KQVKQEQSGT
KSPEKESAQP STVKSPTEAT KDESASLSNT KPLQGEDFQI DGGTFKTPEI DLAKDVFAAL
GTATPAAVAS GKASELVSST ADTTVPPDSA KTEKTQVEEN SKPEETDVKS TPAEVKTVPN
EATQRNVNES KA
