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 24-JAN-2024, entry version 123.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 project:
RT 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 bridges
CC unrelated proteins or stabilizes weak protein-protein complexes in
CC response to calcium. Together with PDCD6, acts as a calcium-dependent
CC adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic
CC reticulum (ER)-Golgi transport by regulating the size of COPII coats.
CC In response to cytosolic calcium increase, the heterodimer formed with
CC PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and
CC SEC31 (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 however
CC unclear: some evidence shows that PEF1 and PDCD6 work together and
CC promote association between PDCD6 and SEC31 in presence of calcium.
CC Other reports show that PEF1 dissociates from PDCD6 in presence of
CC calcium, and may act as a negative regulator of PDCD6 (By similarity).
CC Also acts as a negative regulator of ER-Golgi transport; possibly by
CC inhibiting interaction between PDCD6 and SEC31 (PubMed:27276012).
CC {ECO:0000250|UniProtKB:Q9UBV8, ECO:0000269|PubMed:27276012}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes (via the EF-hand 5) with PDCD6.
CC 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 membrane
CC protein {ECO:0000250|UniProtKB:Q9UBV8}. Note=Membrane-associated in the
CC presence of Ca(2+) (By similarity). Localizes to endoplasmic reticulum
CC exit site (ERES) (PubMed:27276012). {ECO:0000250|UniProtKB:Q9UBV8,
CC 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 AlphaFoldDB; Q641Z8; -.
DR SMR; Q641Z8; -.
DR BioGRID; 255698; 1.
DR IntAct; Q641Z8; 1.
DR STRING; 10116.ENSRNOP00000018742; -.
DR PhosphoSitePlus; Q641Z8; -.
DR jPOST; Q641Z8; -.
DR PaxDb; 10116-ENSRNOP00000018742; -.
DR Ensembl; ENSRNOT00000018742.6; ENSRNOP00000018742.2; ENSRNOG00000013972.7.
DR Ensembl; ENSRNOT00055049067; ENSRNOP00055040373; ENSRNOG00055028334.
DR Ensembl; ENSRNOT00060044823; ENSRNOP00060037174; ENSRNOG00060025889.
DR Ensembl; ENSRNOT00065044371; ENSRNOP00065036395; ENSRNOG00065025728.
DR GeneID; 297900; -.
DR KEGG; rno:297900; -.
DR AGR; RGD:1359536; -.
DR CTD; 553115; -.
DR RGD; 1359536; Pef1.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000155722; -.
DR HOGENOM; CLU_051357_1_0_1; -.
DR InParanoid; Q641Z8; -.
DR OrthoDB; 318691at2759; -.
DR PhylomeDB; Q641Z8; -.
DR TreeFam; TF314682; -.
DR PRO; PR:Q641Z8; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013972; Expressed in adult mammalian kidney and 19 other cell types or tissues.
DR Genevisible; Q641Z8; RN.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum 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:0051592; P:response to calcium ion; ISO:RGD.
DR CDD; cd16184; EFh_PEF_peflin; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR46212; PEFLIN; 1.
DR PANTHER; PTHR46212:SF3; PEFLIN; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Metal-binding; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..283
FT /note="Peflin"
FT /id="PRO_0000247047"
FT REPEAT 21..29
FT /note="1"
FT REPEAT 31..39
FT /note="2"
FT REPEAT 41..48
FT /note="3"
FT REPEAT 49..58
FT /note="4"
FT REPEAT 59..67
FT /note="5"
FT REPEAT 75..83
FT /note="6"
FT REPEAT 84..91
FT /note="7"
FT REPEAT 92..99
FT /note="8"
FT REPEAT 100..108
FT /note="9"
FT DOMAIN 113..148
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 149..179
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 180..215
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 216..252
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 253..282
FT /note="EF-hand 5"
FT /evidence="ECO:0000305"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..108
FT /note="9 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-
FT Y-G-G-P-P"
FT REGION 56..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..283
FT /note="Required for interaction with PDCD6"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV8"
FT COMPBIAS 69..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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
//
