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NCKP1_DANRE
ID   NCKP1_DANRE             Reviewed;        1128 AA.
AC   B0S6R1; B0S6R0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nck-associated protein 1;
DE            Short=NAP 1;
GN   Name=nckap1; ORFNames=si:dkey-234n3.1, wu:fd05c01;
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], AND ALTERNATIVE SPLICING
RP   (ISOFORMS 1 AND 2).
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).
CC   -!- FUNCTION: Part of the WAVE complex that regulates lamellipodia
CC       formation. The WAVE complex regulates actin filament reorganization via
CC       its interaction with the Arp2/3 complex. Actin remodeling activity is
CC       regulated by RAC1 (By similarity). Plays a role in neural tube closure.
CC       {ECO:0000250, ECO:0000250|UniProtKB:Q640K3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection,
CC       lamellipodium membrane {ECO:0000250}; Single-pass membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=At the interface
CC       between the lamellipodial actin meshwork and the membrane.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B0S6R1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B0S6R1-2; Sequence=VSP_038573;
CC   -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAQ13346.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAQ14913.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CR513785; CAQ13346.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX548025; CAQ13346.1; JOINED; Genomic_DNA.
DR   EMBL; CR513785; CAQ13347.1; -; Genomic_DNA.
DR   EMBL; BX548025; CAQ13347.1; JOINED; Genomic_DNA.
DR   EMBL; BX548025; CAQ14913.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CR513785; CAQ14913.1; JOINED; Genomic_DNA.
DR   EMBL; BX548025; CAQ14914.1; -; Genomic_DNA.
DR   EMBL; CR513785; CAQ14914.1; JOINED; Genomic_DNA.
DR   RefSeq; XP_005167980.1; XM_005167923.3. [B0S6R1-1]
DR   RefSeq; XP_005167981.1; XM_005167924.3. [B0S6R1-2]
DR   AlphaFoldDB; B0S6R1; -.
DR   SMR; B0S6R1; -.
DR   STRING; 7955.ENSDARP00000116328; -.
DR   PaxDb; B0S6R1; -.
DR   PeptideAtlas; B0S6R1; -.
DR   PRIDE; B0S6R1; -.
DR   Ensembl; ENSDART00000132696; ENSDARP00000116328; ENSDARG00000060853. [B0S6R1-1]
DR   GeneID; 561894; -.
DR   CTD; 10787; -.
DR   ZFIN; ZDB-GENE-030131-4426; nckap1.
DR   eggNOG; KOG1917; Eukaryota.
DR   GeneTree; ENSGT00390000016619; -.
DR   InParanoid; B0S6R1; -.
DR   OMA; XSIVGMT; -.
DR   OrthoDB; 138196at2759; -.
DR   PhylomeDB; B0S6R1; -.
DR   TreeFam; TF313683; -.
DR   Reactome; R-DRE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-DRE-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DRE-9013404; RAC2 GTPase cycle.
DR   Reactome; R-DRE-9013423; RAC3 GTPase cycle.
DR   PRO; PR:B0S6R1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 9.
DR   Bgee; ENSDARG00000060853; Expressed in early embryo and 27 other tissues.
DR   ExpressionAtlas; B0S6R1; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031209; C:SCAR complex; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:ZFIN.
DR   InterPro; IPR019137; Nck-associated_protein-1.
DR   PANTHER; PTHR12093; PTHR12093; 1.
DR   Pfam; PF09735; Nckap1; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Cell membrane; Cell projection; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1128
FT                   /note="Nck-associated protein 1"
FT                   /id="PRO_0000364439"
FT   TRANSMEM        995..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          640..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         74..75
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038573"
SQ   SEQUENCE   1128 AA;  128741 MW;  14DE4236F8791D63 CRC64;
     MSRGAMQPSQ QKLAEKLTIL NDRGIGMLTR IYNIKKACGD PKAKPSYLID KNLESAVKFI
     VRKFPAVETR NNNQQLAQLQ KEKSEILKNL ALYYFTFVDV MEFKDHVCEL LNTIDACQVF
     FDITVNFDLT KNYLDLVVTY TTLMLLLSRI EERKAIIGLY NYAHEMTHGS SDREYPRLGQ
     MIVDYENPLK KMMEEFVPHG KSLSDALVSL QMVYPRRNLS ADQWRNAQLL SLISAPSTML
     NPAQSDTMPC EYLSLDTMEK WIVFGFILCH AALNSDPAAL SLWKLALQSS TCLCLFRDEV
     FHIHKAAEDL FVNIRGYNKR VNDIRECKES ALSHAGSMHR ERRKFLRSAL KELATVLADQ
     PGLLGPKALF VFMALSFARD EIIWLLRHAD NIQKKSTDDF IDKHIAELIF YMEELRAHVR
     KYGPVMQRYY VQYLSGFDAV VLNELVQNLS VCPEDESIIM SSFVNTMTSL SVKQVEDGEV
     FDFRGMRLDW FRLQAYTSVS KASLGLADHR ELGKMMNTII FHTKMVDSLV EMLVETSDLS
     IFCFYSRAFE KMFQQCLELP SQSRYSISFP LLCTHFMSCT HELCPEERHH IGDRSLSLCN
     MFLDEMAKQA RNLITDICTE QCTLSDQLLP KHCAKTISQA VNKKSKKQTG KKGEPEREKP
     GVESMRKNRL LVTNLDKLHT ALSELCFSIN YVPNMMVWEH TFTPREYLTS HLEIRFTKSI
     VGMTMYNQTT QEIAKPSELL TSVRAYMTVL QSIENYVQID ITRVFNNVLL QQTQHLDSHG
     EPTITSLYTN WYLETLLRQV SNGHIAYFPA MKAFVNLPTE NELTFNAEEY SDISEMRSLS
     ELLGPYGMKF LSESLMWHIS SQVAELKKLV VDNVEVLTQM RTSFDKPDHM AALFKRLTSV
     DSVLKRMTII GVILSFRSLA QEALRDVLSC HIPFLVSSVE DFKDHIPRET DMKVAMNVYE
     LSSAAGLPCE IDPALVVALS SQKSENISPE EEYKIACLLM VFVAVSMPTL ASNVMSQYSP
     AIEGHCNNIH CLAKAINQIA AALFTIHKGS IEDRLKEFLA LASSSLLKIG QETDKTTTRN
     RESVYLLLDM IVQESPFLTM DLLESCFPYV LLRNAYHAVY KQSVSSSA
 
 
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