位置:首页 > 蛋白库 > ARPIN_DANRE
ARPIN_DANRE
ID   ARPIN_DANRE             Reviewed;         226 AA.
AC   Q1LWJ6; Q561T7;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Arpin;
GN   Name=arpin; ORFNames=zgc:112432;
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   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=24132237; DOI=10.1038/nature12611;
RA   Dang I., Gorelik R., Sousa-Blin C., Derivery E., Guerin C., Linkner J.,
RA   Nemethova M., Dumortier J.G., Giger F.A., Chipysheva T.A., Ermilova V.D.,
RA   Vacher S., Campanacci V., Herrada I., Planson A.G., Fetics S., Henriot V.,
RA   David V., Oguievetskaia K., Lakisic G., Pierre F., Steffen A., Boyreau A.,
RA   Peyrieras N., Rottner K., Zinn-Justin S., Cherfils J., Bieche I.,
RA   Alexandrova A.Y., David N.B., Small J.V., Faix J., Blanchoin L.,
RA   Gautreau A.;
RT   "Inhibitory signalling to the Arp2/3 complex steers cell migration.";
RL   Nature 503:281-284(2013).
CC   -!- FUNCTION: Regulates actin polymerization by inhibiting the actin-
CC       nucleating activity of the Arp2/3 complex; the function is competitive
CC       with nucleation promoting factors (By similarity). Involved in steering
CC       cell migration by controlling its directional persistence.
CC       {ECO:0000250, ECO:0000269|PubMed:24132237}.
CC   -!- SUBUNIT: Associates with the Arp2/3 complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}.
CC   -!- DOMAIN: The acidic C-terminus is necessary and sufficient to inhibit
CC       ARP2/3 complex activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Arpin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX548061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093306; AAH93306.1; -; mRNA.
DR   RefSeq; NP_001017780.1; NM_001017780.1.
DR   AlphaFoldDB; Q1LWJ6; -.
DR   SASBDB; Q1LWJ6; -.
DR   STRING; 7955.ENSDARP00000091551; -.
DR   PaxDb; Q1LWJ6; -.
DR   DNASU; 550477; -.
DR   Ensembl; ENSDART00000100778; ENSDARP00000091551; ENSDARG00000041085.
DR   GeneID; 550477; -.
DR   KEGG; dre:550477; -.
DR   CTD; 348110; -.
DR   ZFIN; ZDB-GENE-050417-304; arpin.
DR   eggNOG; ENOG502R4IG; Eukaryota.
DR   GeneTree; ENSGT00530000064251; -.
DR   HOGENOM; CLU_106544_0_0_1; -.
DR   InParanoid; Q1LWJ6; -.
DR   OMA; HLMSSYK; -.
DR   OrthoDB; 1431350at2759; -.
DR   PhylomeDB; Q1LWJ6; -.
DR   PRO; PR:Q1LWJ6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000041085; Expressed in swim bladder and 23 other tissues.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0033058; P:directional locomotion; IDA:UniProtKB.
DR   GO; GO:0051126; P:negative regulation of actin nucleation; IBA:GO_Central.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR   InterPro; IPR018889; Arpin.
DR   PANTHER; PTHR31199; PTHR31199; 1.
DR   Pfam; PF10574; UPF0552; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Arpin"
FT                   /id="PRO_0000424789"
FT   REGION          197..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        100
FT                   /note="Y -> F (in Ref. 2; AAH93306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="F -> S (in Ref. 2; AAH93306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25622 MW;  038896BF253DB046 CRC64;
     MSRIYDNTAL LNKPVHNEKL SFTWDPIVHQ SGHGVILEGT VVDFSRHAIT DVKNRKERYN
     VLYIKPSRVH RRKYDSKGNE IEPNFSDTKK VNTGFLMSSY KVEAKGETDC LDERQLREIV
     NKEQLVKVTI KHCPREAFAF WISEAEMDKT ELEPGQEVRL KTKGDGPFIF SFAKLDSGTV
     TKCNFAGDEN AGASWTEKIM ANKSNQENTG KSAAQGEGAD DDEWDD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024