Entry euk: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   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};
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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   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       113    134       ipfam:EF-hand_5 [T]
FT   MYHIT       105    140       iprf:EF_HAND_2 [T]
FT   MYHIT       172    207       iprf:EF_HAND_2 [T]
FT   MYHIT       185    197       ipat:EF_HAND_1 [T]
FT   MYHIT       109    137       ismart:EFh [T]
FT   MYHIT       118    130       ipat:EF_HAND_1 [T]
FT   MYHIT       177    203       ipfam:EF-hand_6 [T]
FT   MYHIT       176    204       ismart:EFh [T]
FT   MYHIT       146    174       ismart:EFh [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
//