ID PEF1_DANRE Reviewed; 270 AA.
AC Q6DC93;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 10-MAY-2017, entry version 89.
DE RecName: Full=Peflin {ECO:0000250|UniProtKB:Q9UBV8};
DE AltName: Full=PEF protein with a long N-terminal hydrophobic domain {ECO:0000250|UniProtKB:Q9UBV8};
DE AltName: Full=Penta-EF hand domain-containing protein 1 {ECO:0000250|UniProtKB:Q9UBV8};
GN Name=pef1 {ECO:0000250|UniProtKB:Q9UBV8};
GN ORFNames=zgc:100787 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; 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.,
RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA 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., Eliott D., Threadgold G.,
RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA 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.,
RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the
RT human genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-binding protein that acts as an adapter that
CC bridges unrelated proteins or stabilizes weak protein-protein
CC complexes in response to calcium. Acts as a negative regulator of
CC ER-Golgi transport (By similarity). {ECO:0000250|UniProtKB:Q641Z8,
CC ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes (via the EF-hand 5) with
CC pdcd6. {ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBV8}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q641Z8}. Membrane
CC {ECO:0000250|UniProtKB:Q9UBV8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UBV8}. Cytoplasmic vesicle, COPII-coated
CC vesicle membrane {ECO:0000250|UniProtKB:Q9UBV8}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q9UBV8}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CR318592; CAK04964.1; -; Genomic_DNA.
DR EMBL; BC078183; AAH78183.1; -; mRNA.
DR RefSeq; NP_001003643.1; NM_001003643.1.
DR UniGene; Dr.78732; -.
DR ProteinModelPortal; Q6DC93; -.
DR SMR; Q6DC93; -.
DR STRING; 7955.ENSDARP00000033243; -.
DR PaxDb; Q6DC93; -.
DR Ensembl; ENSDART00000032341; ENSDARP00000033243; ENSDARG00000023989.
DR GeneID; 445249; -.
DR KEGG; dre:445249; -.
DR CTD; 553115; -.
DR ZFIN; ZDB-GENE-040801-259; pef1.
DR eggNOG; KOG0037; Eukaryota.
DR eggNOG; ENOG410YKQK; LUCA.
DR GeneTree; ENSGT00620000087734; -.
DR HOGENOM; HOG000231983; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; Q6DC93; -.
DR OMA; CISGMEL; -.
DR OrthoDB; EOG091G0ISY; -.
DR PhylomeDB; Q6DC93; -.
DR TreeFam; TF314682; -.
DR PRO; PR:Q6DC93; -.
DR Proteomes; UP000000437; Chromosome 19.
DR Bgee; ENSDARG00000023989; -.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0060090; F:binding, bridging; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:1902527; P:positive regulation of protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1 270 Peflin.
FT /FTId=PRO_0000247048.
FT REPEAT 22 30 1.
FT REPEAT 44 54 2.
FT REPEAT 62 70 3.
FT REPEAT 72 81 4.
FT REPEAT 83 91 5.
FT DOMAIN 100 135 EF-hand 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 141 169 EF-hand 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 170 202 EF-hand 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 203 239 EF-hand 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 240 269 EF-hand 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT CA_BIND 113 124 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT CA_BIND 180 191 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT REGION 22 91 5 X 9 AA approximate tandem repeat of
FT [AP]-P-G-G-P-Y-G-G-P-P.
FT COMPBIAS 8 92 Gly-rich.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 171 199 ismart:EFh [T]
FT MYHIT 113 125 ipat:EF_HAND_1 [T]
FT MYHIT 180 192 ipat:EF_HAND_1 [T]
FT MYHIT 104 132 ismart:EFh [T]
FT MYHIT 100 135 iprf:EF_HAND_2 [T]
FT MYHIT 141 169 ismart:EFh [T]
FT MYHIT 167 202 iprf:EF_HAND_2 [T]
FT MYHIT 117 166 ipfam:EF-hand_8 [T]
FT MYHIT 172 198 ipfam:EF-hand_6 [T]
SQ SEQUENCE 270 AA; 29425 MW; 575519C11ECDE9BE CRC64;
MSYQYGQGYS GPGGNAPQWQ QPPRAPYAGG PAAGQYGSPY GSAPPGQQYG GGSPYGSYGQ
PGPRAPYGGG QAPGGPYGGY GQPQGGPYRQ QGSAGNVPPG VNPEAYQWFS TVDSDQSGYI
NAKELKQALM NFNNSSFNDE TCIMMLNMFD KTKSGRVDVF GFSALWTFLQ QWRAAFQQFD
RDRSGSINTN EMHQALSQMG YNLSPQFIQE LVNRYSVRGG TGVLQLDRFI QVCTQLQSMT
QAFREKDTGM TGNVRMSYED FLSSAITRLM
//
|
