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CREL2_DANRE
ID   CREL2_DANRE             Reviewed;         341 AA.
AC   Q7SXF6; Q5RFU8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Cysteine-rich with EGF-like domain protein 2;
DE   Flags: Precursor;
GN   Name=creld2; ORFNames=zgc:66383;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=SJD;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possible role in neuronal acetylcholine receptor transport.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR   EMBL; CR751234; CAI20713.1; -; Genomic_DNA.
DR   EMBL; BC055626; AAH55626.1; -; mRNA.
DR   RefSeq; NP_956817.1; NM_200523.1.
DR   AlphaFoldDB; Q7SXF6; -.
DR   STRING; 7955.ENSDARP00000048382; -.
DR   PaxDb; Q7SXF6; -.
DR   PeptideAtlas; Q7SXF6; -.
DR   Ensembl; ENSDART00000048383; ENSDARP00000048382; ENSDARG00000029071.
DR   Ensembl; ENSDART00000193547; ENSDARP00000146751; ENSDARG00000116264.
DR   GeneID; 393495; -.
DR   KEGG; dre:393495; -.
DR   CTD; 79174; -.
DR   ZFIN; ZDB-GENE-040426-1626; creld2.
DR   eggNOG; KOG4260; Eukaryota.
DR   GeneTree; ENSGT00940000160071; -.
DR   HOGENOM; CLU_038974_1_0_1; -.
DR   InParanoid; Q7SXF6; -.
DR   OMA; DQEACVD; -.
DR   OrthoDB; 883628at2759; -.
DR   PhylomeDB; Q7SXF6; -.
DR   TreeFam; TF316507; -.
DR   PRO; PR:Q7SXF6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 4.
DR   Bgee; ENSDARG00000029071; Expressed in tail and 22 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00064; FU; 2.
DR   InterPro; IPR021852; DUF3456.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; LE_dom.
DR   Pfam; PF11938; DUF3456; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00261; FU; 2.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW   Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..341
FT                   /note="Cysteine-rich with EGF-like domain protein 2"
FT                   /id="PRO_0000256248"
FT   DOMAIN          136..178
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          193..248
FT                   /note="FU 1"
FT   REPEAT          254..308
FT                   /note="FU 2"
FT   DOMAIN          291..317
FT                   /note="EGF-like 2; calcium-binding; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        140..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        148..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        168..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CONFLICT        78
FT                   /note="I -> T (in Ref. 2; AAH55626)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="F -> S (in Ref. 2; AAH55626)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   341 AA;  37603 MW;  626565A690D57C07 CRC64;
     MLLSCSIFRL FCIILLLQLG SIYTKDFTAL CSTCRQLVDD FDKGLEKTAK QNFGGGNTAW
     EERKLSKYET SEIRLTEILE GLCQSSNFEC SHMLEENEEH LEAWWFKRKT KHPDLFKWFC
     IETIKVCCPK GSFGPDCNTC IGGADRPCHG NGKCDGDGTR AGNGKCSCDE GYDGEFCLDC
     SDGYFNSLRN DTFFLCKECH ESCVGCSGGT NQHCKECRNG WVKDQEGSCI DINECIKDPA
     PCSDDQYCLN TDGSFSCKAC DIRCTGCKGD GASSCLNCAD GYKDEEGTCT DIDECTEDPA
     SCSDNQHCLN TDGSFSCEEK VPAFNSEGAK TGDSPEKHED L
 
 
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