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 10-MAY-2017, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: 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
RT expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250|UniProtKB:Q641Z8,
CC ECO:0000250|UniProtKB:Q9UBV8}.
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: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}. Note=Membrane-
CC associated in the presence of Ca(2+) (By similarity). Localizes to
CC endoplasmic reticulum exit site (ERES) (By similarity).
CC {ECO:0000250|UniProtKB:Q641Z8, 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; Positions=248; Evidence={ECO:0000305};
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; 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 UniGene; Mm.20818; -.
DR ProteinModelPortal; Q8BFY6; -.
DR SMR; Q8BFY6; -.
DR STRING; 10090.ENSMUSP00000030563; -.
DR PhosphoSitePlus; Q8BFY6; -.
DR EPD; Q8BFY6; -.
DR MaxQB; Q8BFY6; -.
DR PaxDb; Q8BFY6; -.
DR PeptideAtlas; Q8BFY6; -.
DR PRIDE; Q8BFY6; -.
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 eggNOG; KOG0037; Eukaryota.
DR eggNOG; ENOG410YKQK; LUCA.
DR GeneTree; ENSGT00620000087734; -.
DR HOGENOM; HOG000231983; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; Q8BFY6; -.
DR OMA; FTNSNAM; -.
DR OrthoDB; EOG091G0ISY; -.
DR PhylomeDB; Q8BFY6; -.
DR TreeFam; TF314682; -.
DR PRO; PR:Q8BFY6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR Bgee; ENSMUSG00000028779; -.
DR CleanEx; MM_PEF1; -.
DR Genevisible; Q8BFY6; MM.
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; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
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:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
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; ISO:MGI.
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; 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; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Isopeptide bond; Membrane; Metal-binding;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1 275 Peflin.
FT /FTId=PRO_0000247046.
FT REPEAT 21 29 1.
FT REPEAT 31 39 2.
FT REPEAT 41 49 3.
FT REPEAT 50 59 4.
FT REPEAT 60 68 5.
FT REPEAT 76 84 6.
FT REPEAT 85 91 7.
FT REPEAT 92 100 8.
FT DOMAIN 105 140 EF-hand 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 146 174 EF-hand 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 172 207 EF-hand 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 208 244 EF-hand 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT DOMAIN 245 274 EF-hand 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT CA_BIND 118 129 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT CA_BIND 185 196 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00448}.
FT REGION 21 100 8 X 9 AA approximate tandem repeat of
FT [AP]-P-G-G-P-Y-G-G-P-P.
FT REGION 195 275 Required for interaction with PDCD6.
FT {ECO:0000250|UniProtKB:Q9UBV8}.
FT CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT {ECO:0000250|UniProtKB:Q9UBV8}.
FT CONFLICT 148 148 L -> H (in Ref. 2; AAH19191).
FT {ECO:0000305}.
FT CONFLICT 218 218 S -> F (in Ref. 1; BAB28735).
FT {ECO:0000305}.
FT CONFLICT 257 257 G -> R (in Ref. 1; BAB25010).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 172 207 iprf:EF_HAND_2 [T]
FT MYHIT 146 174 ismart:EFh [T]
FT MYHIT 105 140 iprf:EF_HAND_2 [T]
FT MYHIT 113 134 ipfam:EF-hand_5 [T]
FT MYHIT 109 137 ismart:EFh [T]
FT MYHIT 176 204 ismart:EFh [T]
FT MYHIT 118 130 ipat:EF_HAND_1 [T]
FT MYHIT 177 203 ipfam:EF-hand_6 [T]
FT MYHIT 185 197 ipat:EF_HAND_1 [T]
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
//
|
