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Database: UniProt
Entry: Q6GQB1_XENLA
LinkDB: Q6GQB1_XENLA
Original site: Q6GQB1_XENLA 
ID   Q6GQB1_XENLA            Unreviewed;      1177 AA.
AC   Q6GQB1;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=MGC80200 protein {ECO:0000313|EMBL:AAH72835.1};
DE   SubName: Full=Neuronal cell adhesion molecule L homeolog precursor {ECO:0000313|RefSeq:NP_001085487.1};
GN   Name=nrcam.L {ECO:0000313|RefSeq:NP_001085487.1,
GN   ECO:0000313|Xenbase:XB-GENE-865900};
GN   Synonyms=MGC80200 {ECO:0000313|EMBL:AAH72835.1}, nrcam
GN   {ECO:0000313|RefSeq:NP_001085487.1,
GN   ECO:0000313|Xenbase:XB-GENE-865900};
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 {ECO:0000313|EMBL:AAH72835.1};
RN   [1] {ECO:0000313|RefSeq:NP_001085487.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH72835.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH72835.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001085487.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27942869;
RA   Lokapally A., Metikala S., Hollemann T.;
RT   "Xenopus laevis neuronal cell adhesion molecule (nrcam): plasticity of a
RT   CAM in the developing nervous system.";
RL   Dev. Genes Evol. 227:61-67(2017).
RN   [4] {ECO:0000313|RefSeq:NP_001085487.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR   EMBL; BC072835; AAH72835.1; -; mRNA.
DR   RefSeq; NP_001085487.1; NM_001092018.1.
DR   GeneID; 443913; -.
DR   KEGG; xla:443913; -.
DR   AGR; Xenbase:XB-GENE-865900; -.
DR   CTD; 443913; -.
DR   Xenbase; XB-GENE-865900; nrcam.L.
DR   OrthoDB; 2912783at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 443913; Expressed in brain and 3 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd05874; IgI_NrCAM; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; IPR026966; Neurofascin/L1/NrCAM_C.
DR   PANTHER; PTHR44170:SF15; NEURONAL CELL ADHESION MOLECULE; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF13882; Bravo_FIGEY; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 6.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   2: Evidence at transcript level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001085487.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1177
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001085487.1"
FT                   /id="PRO_5033206785"
FT   TRANSMEM        1042..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..123
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          134..224
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          262..347
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          350..437
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          443..529
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          533..620
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          627..722
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          724..821
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          826..928
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          932..1028
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          707..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1072..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1072..1128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1177 AA;  130925 MW;  0C1C005089D4079F CRC64;
     MQEKKSTFPK RASLVLFLCQ VITALEVPLD LLQPPTITHQ SPKNYIVDPR ESIVIQCEAK
     GKPPPSFSWT RNGTHFDIDK DPYVTMKPNS GTLVINTMNG ARVDAYEGEY QCTARNDRGS
     ALSNNIVIRQ SRSPLWTKEK IEPIVLQQGV PLVLPCNPPK GLPPPIIFWM DNSFQKLPQN
     KRVSQGLNGD LYFSNVQPED TRDFYICYAR FNLTQTIHQK QPISLKVLTM DGLNETIAAN
     LSDTEFYGDS PAGERRPSML FPNMTASNKT VLLGEVLLLE CIAEGLPTPE IHWRKESADL
     PAGRVFYENF NKTLRIIDVT EADAGKYKCI GRNILGTTHH IITVNVKSSP YWISPPTNIV
     LSPGEDGSLI CRASGNPTPS ITWLINGVSI ELAPTDASRR VDGDTIIFSK VQDGATAVYQ
     CNVSNKYGYL LANAFVNVLA EPPRIMVLKH VYKVIANNVA LLHCPFFGSP KPEIKWFKGV
     HGSILHGNGY VFHDNGTLEI PVAQKDSSGN YTCVATNTFG SVKDMIGLQI KDPTMIIKQP
     EYRVIQRYGS AHFECRVKHD PTLKPVVLWL KDDSELLNDE RFKMTKGHLT IKNVTEKDEG
     TYTCVANTDL DTVSASAVLT VVDRPNHPFD LELTDHHERS VQLSWVPGDD NNSPITNFMI
     EYEDAMHDPG IWHFQAKVSG TQTTATLSLS PFVNYSFRVI AVNEIGSSDP SESSEQYMTK
     PAEPDKNPSG IKGVGTEPDN LVIAWEPIKG FDSNGPGLQY KVSWRQKDFD DEWTSIIVAN
     VSKYIVSGTP TFEPYEIKVQ ALNDIGYAPD PSVIIGYSGE DLPMTAPSNV EVEVINNTLA
     KVQWESAPST SIRGHLQGYR VYYWKAENQT KRNKRHMEKH MLSFHGNKTH GMLPGLEPFK
     SYIVNVRVFN GKGEGPPSTD KYFETPEGVP SAPLKLDIVE RTIDSLTLMW KPPAHPNGVL
     TQYTLIFQSI NATHELSPPV EITIPTNETS LVLRNLNQST RYKFYLYANT AVGPGIQITQ
     EAITALDQAM ASRQVDIATQ GWFIGLMCAV ALLILVLLII CFIRRNKGGK YPVKEKEDAH
     ADPEIQPMKE DDGTFGEYSD AEDHKPLKKG SRTPSDRTVK KDDSDDSLVD YGEGVNGQFN
     EDGSFIGQYS GKKEKEPVEG NESSEAPSPV NAMNSFV
//
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