PEF1_XENLA
ID PEF1_XENLA Reviewed; 283 AA.
AC Q5PQ53;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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. Acts as a negative regulator of ER-Golgi transport
CC (By similarity). {ECO:0000250|UniProtKB:Q641Z8,
CC ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes (via the EF-hand 5) with pdcd6.
CC {ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- INTERACTION:
CC Q5PQ53; Q4A520: XB5813854.L; NbExp=8; IntAct=EBI-8160818, EBI-8160800;
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 membrane
CC protein {ECO:0000250|UniProtKB:Q9UBV8}.
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DR EMBL; BC087356; AAH87356.1; -; mRNA.
DR RefSeq; NP_001088714.1; NM_001095245.1.
DR AlphaFoldDB; Q5PQ53; -.
DR SMR; Q5PQ53; -.
DR IntAct; Q5PQ53; 1.
DR MINT; Q5PQ53; -.
DR DNASU; 495978; -.
DR GeneID; 495978; -.
DR KEGG; xla:495978; -.
DR CTD; 495978; -.
DR Xenbase; XB-GENE-1013241; pef1.L.
DR OMA; YNKSYNP; -.
DR OrthoDB; 1330600at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 495978; Expressed in internal ear and 19 other tissues.
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:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 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; PF13499; EF-hand_7; 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 1: Evidence at protein level;
KW Calcium; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..283
FT /note="Peflin"
FT /id="PRO_0000247049"
FT REPEAT 21..30
FT /note="1"
FT REPEAT 36..44
FT /note="2"
FT REPEAT 45..54
FT /note="3"
FT REPEAT 55..62
FT /note="4"
FT REPEAT 71..79
FT /note="5"
FT REPEAT 80..87
FT /note="6"
FT REPEAT 88..95
FT /note="7"
FT REPEAT 96..104
FT /note="8"
FT DOMAIN 113..148
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 154..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 21..104
FT /note="8 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-
FT Y-G-G-P-P"
FT REGION 37..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Polar 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; 30533 MW; 129F451E202CBE1F CRC64;
MASYPYGQGY HGAAGQPPGA PQTNYYGGQQ YGGGVQPAAS YGRPAPGAPY GSPPSGGVYG
HPVPGSAAPG APGGPYGGQA PGGPYSVPGS TPYGSQQHGS YGQGAPAGNI PPGVDPEAFS
WFQTVDTDHS GYISLKELKQ ALVNTNWSSF NDETCTMMMN MFDKSNSGRI DMFGFSALWR
FIQQWRNLFQ QYDRDRSGSI NQGELHQALC QMGYQLSPQF VQIVMSRYAQ RSAQPGLQLD
RFIQICTQLQ SMTEAFREKD TGQIGTAKLS YEDFITMTTT RLL
