Legends: 1, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). {ECO:0000250|UniProtKB:Q9UBV8}; 2, REPEAT 1; 3, REPEAT 2; 4, REPEAT 3; 5, REPEAT 4; 6, REPEAT 5; 7, REPEAT 6; 8, REPEAT 7; 9, REPEAT 8; 10, REPEAT 9; 11, EF-hand 1. {ECO:0000255|PROSITE- ProRule:PRU00448}; 12, EF-hand 2. {ECO:0000255|PROSITE- ProRule:PRU00448}; 13, EF-hand 3. {ECO:0000255|PROSITE- ProRule:PRU00448}; 14, EF-hand 4. {ECO:0000255|PROSITE- ProRule:PRU00448}; 15, EF-hand 5. {ECO:0000255|PROSITE- ProRule:PRU00448}; 16, CA_BIND 1. {ECO:0000255|PROSITE- ProRule:PRU00448}; 17, CA_BIND 2. {ECO:0000255|PROSITE- ProRule:PRU00448}; 18, REGION 9 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-Y-G-G-P-P; 19, REGION Required for interaction with PDCD6. {ECO:0000250|UniProtKB:Q9UBV8}; 20, iprf:EF_HAND_2 [T]; 21, ipat:EF_HAND_1 [T]; 22, ismart:EFh [T]; 23, ipfam:EF-hand_5 [T]; 24, ipfam:EF-hand_6 [T].
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ID PEF1_RAT Reviewed; 283 AA.
AC Q641Z8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 10-MAY-2017, entry version 92.
DE RecName: Full=Peflin {ECO:0000303|PubMed:15489334};
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:0000312|RGD:1359536};
GN Name=Pef1 {ECO:0000312|RGD:1359536};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27276012; DOI=10.1371/journal.pone.0157227;
RA Rayl M., Truitt M., Held A., Sargeant J., Thorsen K., Hay J.C.;
RT "Penta-EF-Hand protein peflin is a negative regulator of ER-to-Golgi
RT transport.";
RL PLoS ONE 11:E0157227-E0157227(2016).
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. Together with PDCD6, acts as
CC calcium-dependent adapter for the BCR(KLHL12) complex, a complex
CC involved in endoplasmic reticulum (ER)-Golgi transport by
CC regulating the size of COPII coats. In response to cytosolic
CC calcium increase, the heterodimer formed with PDCD6 interacts
CC with, and bridges together the BCR(KLHL12) complex and SEC31
CC (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and
CC subsequent collagen export, which is required for neural crest
CC specification. Its role in the heterodimer formed with PDCD6 is
CC however unclear: some evidences show that PEF1 and PDCD6 work
CC together and promote association between PDCD6 and SEC31 in
CC presence of calcium. Other reports show that PEF1 dissociates from
CC PDCD6 in presence of calcium, and may act as a negative regulator
CC of PDCD6 (By similarity). Also acts as a negative regulator of ER-
CC Golgi transport; possibly by inhibiting interaction between PDCD6
CC and SEC31 (PubMed:27276012). {ECO:0000250|UniProtKB:Q9UBV8,
CC ECO:0000269|PubMed:27276012}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes (via the EF-hand 5) with
CC PDCD6. Dissociates from PDCD6 in presence of calcium.
CC {ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBV8}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:27276012}. Membrane
CC {ECO:0000269|PubMed:27276012}; 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}. Note=Membrane-
CC associated in the presence of Ca(2+) (By similarity). Localizes to
CC endoplasmic reticulum exit site (ERES) (PubMed:27276012).
CC {ECO:0000250|UniProtKB:Q9UBV8, ECO:0000269|PubMed:27276012}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex.
CC {ECO:0000250|UniProtKB:Q9UBV8}.
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DR EMBL; BC082028; AAH82028.1; -; mRNA.
DR RefSeq; NP_001007652.1; NM_001007651.1.
DR UniGene; Rn.96097; -.
DR ProteinModelPortal; Q641Z8; -.
DR SMR; Q641Z8; -.
DR STRING; 10116.ENSRNOP00000018742; -.
DR PaxDb; Q641Z8; -.
DR PRIDE; Q641Z8; -.
DR Ensembl; ENSRNOT00000018742; ENSRNOP00000018742; ENSRNOG00000013972.
DR GeneID; 297900; -.
DR KEGG; rno:297900; -.
DR CTD; 553115; -.
DR RGD; 1359536; Pef1.
DR eggNOG; KOG0037; Eukaryota.
DR eggNOG; ENOG410YKQK; LUCA.
DR GeneTree; ENSGT00620000087734; -.
DR HOGENOM; HOG000231983; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; Q641Z8; -.
DR OMA; PSMQLDR; -.
DR OrthoDB; EOG091G0ISY; -.
DR PhylomeDB; Q641Z8; -.
DR TreeFam; TF314682; -.
DR PRO; PR:Q641Z8; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013972; -.
DR Genevisible; Q641Z8; RN.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
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:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
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 GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13405; EF-hand_6; 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; Isopeptide bond; Membrane; Metal-binding;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 283 Peflin.
FT /FTId=PRO_0000247047.
FT REPEAT 21 29 1.
FT REPEAT 31 39 2.
FT REPEAT 41 48 3.
FT REPEAT 49 58 4.
FT REPEAT 59 67 5.
FT REPEAT 75 83 6.
FT REPEAT 84 91 7.
FT REPEAT 92 99 8.
FT REPEAT 100 108 9.
FT DOMAIN 113 148 EF-hand 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 149 179 EF-hand 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 180 215 EF-hand 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 216 252 EF-hand 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 253 282 EF-hand 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT CA_BIND 126 137 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT CA_BIND 193 204 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT REGION 21 108 9 X 9 AA approximate tandem repeat of
FT [AP]-P-G-G-P-Y-G-G-P-P.
FT REGION 203 283 Required for interaction with PDCD6.
FT {ECO:0000250|UniProtKB:Q9UBV8}.
FT CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT {ECO:0000250|UniProtKB:Q9UBV8}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 113 148 iprf:EF_HAND_2 [T]
FT MYHIT 193 205 ipat:EF_HAND_1 [T]
FT MYHIT 126 138 ipat:EF_HAND_1 [T]
FT MYHIT 184 212 ismart:EFh [T]
FT MYHIT 154 182 ismart:EFh [T]
FT MYHIT 180 215 iprf:EF_HAND_2 [T]
FT MYHIT 117 145 ismart:EFh [T]
FT MYHIT 121 142 ipfam:EF-hand_5 [T]
FT MYHIT 185 211 ipfam:EF-hand_6 [T]
SQ SEQUENCE 283 AA; 30012 MW; 2454D005C02C595D CRC64;
MASYPDGQSY PGAAGQVPGP HPGGYYPGPP HGGGQYGSGF PPGGYGAPAP GGPYGYPSAG
GTPSGTPGGP YGGGPPGGPY GGGPPGGPYG QAHPSPYGTQ PPGPYGQGGV PPNVDPEAYS
WFQSVDADHS GYISLKELKQ ALVNSNWSSF NDETCLMMIN MFDKTKTGRI DVVGFSALWK
FLQQWKNLFQ QYDRDHSGSI SSTELQQALS QMGYNLSPQF TQLLVSRYCT RSAIPAMQLD
CFIKVCTQLQ VLTEAFREKD TAVQGNIRLS FEDFVTMTAS RML
//
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