PEF1_MOUSE
ID PEF1_MOUSE Reviewed; 275 AA.
AC Q8BFY6; Q8VCT5; Q9CYW8; Q9D934;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
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:0000312|MGI:MGI:1915148};
GN Name=Pef1 {ECO:0000312|MGI:MGI:1915148};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q641Z8, ECO:0000250|UniProtKB:Q9UBV8}.
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: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}. Note=Membrane-associated in the
CC presence of Ca(2+) (By similarity). Localizes to endoplasmic reticulum
CC exit site (ERES) (By similarity). {ECO:0000250|UniProtKB:Q641Z8,
CC ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex.
CC {ECO:0000250|UniProtKB:Q9UBV8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28735.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK007394; BAB25010.1; -; mRNA.
DR EMBL; AK013238; BAB28735.1; ALT_FRAME; mRNA.
DR EMBL; AK046247; BAC32654.1; -; mRNA.
DR EMBL; AK075978; BAC36091.1; -; mRNA.
DR EMBL; BC019191; AAH19191.1; -; mRNA.
DR CCDS; CCDS18706.1; -.
DR RefSeq; NP_080717.2; NM_026441.4.
DR AlphaFoldDB; Q8BFY6; -.
DR SMR; Q8BFY6; -.
DR BioGRID; 212522; 29.
DR STRING; 10090.ENSMUSP00000112638; -.
DR PhosphoSitePlus; Q8BFY6; -.
DR SwissPalm; Q8BFY6; -.
DR EPD; Q8BFY6; -.
DR jPOST; Q8BFY6; -.
DR MaxQB; Q8BFY6; -.
DR PaxDb; Q8BFY6; -.
DR PeptideAtlas; Q8BFY6; -.
DR PRIDE; Q8BFY6; -.
DR ProteomicsDB; 289345; -.
DR Antibodypedia; 31143; 169 antibodies from 28 providers.
DR DNASU; 67898; -.
DR Ensembl; ENSMUST00000030563; ENSMUSP00000030563; ENSMUSG00000028779.
DR Ensembl; ENSMUST00000118199; ENSMUSP00000112638; ENSMUSG00000028779.
DR GeneID; 67898; -.
DR KEGG; mmu:67898; -.
DR UCSC; uc008uyw.1; mouse.
DR CTD; 553115; -.
DR MGI; MGI:1915148; Pef1.
DR VEuPathDB; HostDB:ENSMUSG00000028779; -.
DR eggNOG; KOG0037; Eukaryota.
DR GeneTree; ENSGT00940000155722; -.
DR HOGENOM; CLU_051357_1_0_1; -.
DR InParanoid; Q8BFY6; -.
DR OMA; YNKSYNP; -.
DR OrthoDB; 1330600at2759; -.
DR PhylomeDB; Q8BFY6; -.
DR TreeFam; TF314682; -.
DR BioGRID-ORCS; 67898; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Pef1; mouse.
DR PRO; PR:Q8BFY6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BFY6; protein.
DR Bgee; ENSMUSG00000028779; Expressed in granulocyte and 256 other tissues.
DR Genevisible; Q8BFY6; MM.
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:MGI.
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:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
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:MGI.
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; Ubl conjugation.
FT CHAIN 1..275
FT /note="Peflin"
FT /id="PRO_0000247046"
FT REPEAT 21..29
FT /note="1"
FT REPEAT 31..39
FT /note="2"
FT REPEAT 41..49
FT /note="3"
FT REPEAT 50..59
FT /note="4"
FT REPEAT 60..68
FT /note="5"
FT REPEAT 76..84
FT /note="6"
FT REPEAT 85..91
FT /note="7"
FT REPEAT 92..100
FT /note="8"
FT DOMAIN 105..140
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 146..174
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 172..207
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 208..244
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 245..274
FT /note="EF-hand 5"
FT /evidence="ECO:0000305"
FT REGION 21..100
FT /note="8 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-
FT Y-G-G-P-P"
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..275
FT /note="Required for interaction with PDCD6"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV8"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 148
FT /note="L -> H (in Ref. 2; AAH19191)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="S -> F (in Ref. 1; BAB28735)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="G -> R (in Ref. 1; BAB25010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 29228 MW; DE4782B47ABEE9E2 CRC64;
MASYPNGQSC PGAAGQVPGV PPGGYYPGPP HGGGQYGSGL PPGGGYGAPA PGGPYGYPSA
GGVPSGTPSG PYGGIPPGGP YGQLPPGGPY GTQPGHYGQG GVPPNVDPEA YSWFQSVDAD
HSGYISLKEL KQALVNSNWS SFNDETCLMM INMFDKTKSG RIDVAGFSAL WKFLQQWRNL
FQQYDRDRSG SISSTELQQA LSQMGYNLSP QFTQLLVSRY CARSAIPAMQ LDCFIKVCTQ
LQVLTEAFRE KDTAVQGNIR LSFEDFVTMT ASRML
