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Database: UniProt
Entry: A0A3P9P2T6_POERE
LinkDB: A0A3P9P2T6_POERE
Original site: A0A3P9P2T6_POERE 
ID   A0A3P9P2T6_POERE        Unreviewed;      1202 AA.
AC   A0A3P9P2T6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Neural cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSPREP00000016146.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000016146.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000016146.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000016146.1};
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_008423202.1; XM_008424980.2.
DR   AlphaFoldDB; A0A3P9P2T6; -.
DR   Ensembl; ENSPRET00000016314.1; ENSPREP00000016146.1; ENSPREG00000010771.1.
DR   GeneID; 103474177; -.
DR   CTD; 114442; -.
DR   GeneTree; ENSGT00940000155743; -.
DR   OrthoDB; 5233206at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000010771; Expressed in head.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00096; Ig; 2.
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; 4.
DR   Pfam; PF13927; Ig_3; 1.
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:UP000242638};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1202
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018054999"
FT   TRANSMEM        716..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..110
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          115..202
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          209..295
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          302..405
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          410..498
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          504..602
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          604..700
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          584..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1110..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..876
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..907
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..975
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1046
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1202 AA;  130599 MW;  3FA56DB11570DE47 CRC64;
     MVQTRNVFLA LLLVGSTVSL EVQITPTHGE ISLGESKFFM CDVVGVAKHV DWYGPSGERI
     APNRPDLTVT RNDESSSTLT FYEAKTDSAG TYKCVATNGD QQAEATVKVK IFQRITFTNA
     PPRQEFTEGD NANIVCDVTS SPPPTVFWKY KGAKIQMEKD VRFKVLSNNH LQIRGIKKTD
     EGMYMCEARL MARGEIDLRP ISVVVNVLPT IRIWQSEVNA TAEVAQPATL TCAVDGYPEP
     MVTWIRNGVE LRDEEKYGFN EDGSEMTIMD VTKLDEGEYT CVAKNKAGES EKELSLRVFV
     KPKITYIVNR TASETEEQVT VTCEASGDPT PTISWSYGEQ VFTEGDQASW TRPEQHKSPD
     GNVVVRSDAR VSSLTLKYVK YTDAGQYLCT ARSAIGEDEQ TAYLEVRYTP KIHGTVAVYT
     WEGNPVNISC EVKAFPTDVS IVWLRDGLQL PNSNTTNIKI FRTPLSSYLQ ITPESENDFG
     SYNCTASNEM GTESKEFLLI QAEVPSSLVI DEVRPFSTTA LIQFGEPEST GGVPVLKYRA
     EWRMQGRSSW TQKVYEVQDD FVNEVTITGL KPESRYEVKL SAINGKGEGE SSPTERFKTE
     PVRNPNPPKL EGSVEPKGNS LKVSWLKQDD GGSPILHYLI RYKPIQTSQW KPEIRMPSGS
     DYVVLRGLDW DTEYDVYVVA ENLKGKSPPA TMSFRTSAEP EAFPDMGDEG PFFMNIILWA
     GILVVVFVLL LLAVDVTCYF VNKCGLIMCL CGKSGTGTKG HVLEEGKAAF VKDESKEPIV
     EVRTEDECTA NHNAAGPIEP NETTPLTKPE LVASLALDTP SSVATNSDTA TATIDPAQES
     PSSETTTLTC SLSTLANEPS PTPLTAPAPT PESNTAPPTP VVSSTAVEAK MAPLLEERGR
     KTSEEPEKTS NPPATPEQCR PQKSGTPIPP KRRHSPKLAA LNAKNSPPVS PLAVSSPPPI
     PDGKKPAPSP PVNKPTPRAN AVALSKETLA QTAATTANTA LPKPDPESKP GLPDSTAYTF
     TDFDTDNPTG NNIPTPKPTT INAPSDIPNA VEDPYLKNPI TLLADIPSPL PITAIALAVP
     NDLLIPGSDL YDLTAPDGVH KNADLELELR NGAGRPSRPR SDLINLESPS AAPSLPSGDQ
     ADFPPSGPVL EASETLKTAP PVNDEKIFAD EKSKLEEGDL PNPLITSAHN SVIQTNTTES
     KV
//
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