Full text data of PEF1
PEF1
(ABP32)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Peflin (PEF protein with a long N-terminal hydrophobic domain; Penta-EF hand domain-containing protein 1)
Peflin (PEF protein with a long N-terminal hydrophobic domain; Penta-EF hand domain-containing protein 1)
hRBCD
IPI00018235
IPI00018235 Peflin Peflin membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00018235 Peflin Peflin membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q9UBV8
ID PEF1_HUMAN Reviewed; 284 AA.
AC Q9UBV8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Peflin;
DE AltName: Full=PEF protein with a long N-terminal hydrophobic domain;
DE AltName: Full=Penta-EF hand domain-containing protein 1;
GN Name=PEF1; Synonyms=ABP32; ORFNames=UNQ1845/PRO3573;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10486255; DOI=10.1006/bbrc.1999.1189;
RA Kitaura Y., Watanabe M., Satoh H., Kawai T., Hitomi K., Maki M.;
RT "Peflin, a novel member of the five-EF-hand-protein family, is similar
RT to the apoptosis-linked gene 2 (ALG-2) protein but possesses
RT nonapeptide repeats in the N-terminal hydrophobic region.";
RL Biochem. Biophys. Res. Commun. 263:68-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Shibata M., Noguchi J.;
RT "A putative calcium binding protein that has five EF-hand motifs.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Skin;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6.
RX PubMed=11278427; DOI=10.1074/jbc.M008649200;
RA Kitaura Y., Matsumoto S., Satoh H., Hitomi K., Maki M.;
RT "Peflin and ALG-2, members of the penta-EF-hand protein family, form a
RT heterodimer that dissociates in a Ca2+-dependent manner.";
RL J. Biol. Chem. 276:14053-14058(2001).
RN [8]
RP INTERACTION WITH PDCD6.
RX PubMed=11883899; DOI=10.1006/abbi.2001.2736;
RA Kitaura Y., Satoh H., Takahashi H., Shibata H., Maki M.;
RT "Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized
RT by dimerization through their fifth EF-hand regions.";
RL Arch. Biochem. Biophys. 399:12-18(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PDCD6. Dissociates from
CC PDCD6 in presence of Ca(2+).
CC -!- INTERACTION:
CC Q15038:DAZAP2; NbExp=3; IntAct=EBI-724639, EBI-724310;
CC Q53G59:KLHL12; NbExp=2; IntAct=EBI-724639, EBI-740929;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Note=Membrane-associated in the presence of Ca(2+).
CC -!- SIMILARITY: Contains 5 EF-hand domains.
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; AB026628; BAA85163.1; -; mRNA.
DR EMBL; AB018357; BAA84922.1; -; mRNA.
DR EMBL; AY359011; AAQ89370.1; -; mRNA.
DR EMBL; AK001420; BAA91680.1; -; mRNA.
DR EMBL; CR542139; CAG46936.1; -; mRNA.
DR EMBL; BC002773; AAH02773.1; -; mRNA.
DR EMBL; BC012561; AAH12561.1; -; mRNA.
DR RefSeq; NP_036524.1; NM_012392.3.
DR UniGene; Hs.470417; -.
DR ProteinModelPortal; Q9UBV8; -.
DR SMR; Q9UBV8; 123-278.
DR IntAct; Q9UBV8; 11.
DR MINT; MINT-5003645; -.
DR STRING; 9606.ENSP00000362807; -.
DR PhosphoSite; Q9UBV8; -.
DR DMDM; 74761895; -.
DR REPRODUCTION-2DPAGE; IPI00018235; -.
DR PaxDb; Q9UBV8; -.
DR PRIDE; Q9UBV8; -.
DR DNASU; 553115; -.
DR Ensembl; ENST00000373703; ENSP00000362807; ENSG00000162517.
DR GeneID; 553115; -.
DR KEGG; hsa:553115; -.
DR UCSC; uc001bth.2; human.
DR CTD; 553115; -.
DR GeneCards; GC01M032095; -.
DR HGNC; HGNC:30009; PEF1.
DR MIM; 610033; gene.
DR neXtProt; NX_Q9UBV8; -.
DR PharmGKB; PA142671184; -.
DR eggNOG; NOG249191; -.
DR HOGENOM; HOG000231983; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; Q9UBV8; -.
DR OMA; FLQGCPG; -.
DR OrthoDB; EOG7RV9FM; -.
DR PhylomeDB; Q9UBV8; -.
DR GeneWiki; PEF1; -.
DR GenomeRNAi; 553115; -.
DR NextBio; 112375; -.
DR PRO; PR:Q9UBV8; -.
DR ArrayExpress; Q9UBV8; -.
DR Bgee; Q9UBV8; -.
DR CleanEx; HS_PEF1; -.
DR Genevestigator; Q9UBV8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0051592; P:response to calcium ion; IPI:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 3.
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; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1 284 Peflin.
FT /FTId=PRO_0000247045.
FT REPEAT 21 29 1.
FT REPEAT 31 39 2.
FT REPEAT 41 49 3.
FT REPEAT 50 58 4.
FT REPEAT 59 67 5.
FT REPEAT 76 84 6.
FT REPEAT 85 92 7.
FT REPEAT 93 100 8.
FT REPEAT 101 109 9.
FT DOMAIN 114 149 EF-hand 1.
FT DOMAIN 155 183 EF-hand 2.
FT DOMAIN 181 216 EF-hand 3.
FT DOMAIN 217 253 EF-hand 4.
FT DOMAIN 254 283 EF-hand 5.
FT CA_BIND 127 138 1 (Potential).
FT CA_BIND 194 205 2 (Potential).
FT REGION 21 109 9 X 9 AA approximate tandem repeat of
FT [AP]-P-G-G-P-Y-G-G-P-P.
FT REGION 204 284 Required for interaction with PDCD6.
SQ SEQUENCE 284 AA; 30381 MW; 2E9AA5750CB7A68A CRC64;
MASYPYRQGC PGAAGQAPGA PPGSYYPGPP NSGGQYGSGL PPGGGYGGPA PGGPYGPPAG
GGPYGHPNPG MFPSGTPGGP YGGAAPGGPY GQPPPSSYGA QQPGLYGQGG APPNVDPEAY
SWFQSVDSDH SGYISMKELK QALVNCNWSS FNDETCLMMI NMFDKTKSGR IDVYGFSALW
KFIQQWKNLF QQYDRDRSGS ISYTELQQAL SQMGYNLSPQ FTQLLVSRYC PRSANPAMQL
DRFIQVCTQL QVLTEAFREK DTAVQGNIRL SFEDFVTMTA SRML
//
ID PEF1_HUMAN Reviewed; 284 AA.
AC Q9UBV8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Peflin;
DE AltName: Full=PEF protein with a long N-terminal hydrophobic domain;
DE AltName: Full=Penta-EF hand domain-containing protein 1;
GN Name=PEF1; Synonyms=ABP32; ORFNames=UNQ1845/PRO3573;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10486255; DOI=10.1006/bbrc.1999.1189;
RA Kitaura Y., Watanabe M., Satoh H., Kawai T., Hitomi K., Maki M.;
RT "Peflin, a novel member of the five-EF-hand-protein family, is similar
RT to the apoptosis-linked gene 2 (ALG-2) protein but possesses
RT nonapeptide repeats in the N-terminal hydrophobic region.";
RL Biochem. Biophys. Res. Commun. 263:68-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Shibata M., Noguchi J.;
RT "A putative calcium binding protein that has five EF-hand motifs.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Skin;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6.
RX PubMed=11278427; DOI=10.1074/jbc.M008649200;
RA Kitaura Y., Matsumoto S., Satoh H., Hitomi K., Maki M.;
RT "Peflin and ALG-2, members of the penta-EF-hand protein family, form a
RT heterodimer that dissociates in a Ca2+-dependent manner.";
RL J. Biol. Chem. 276:14053-14058(2001).
RN [8]
RP INTERACTION WITH PDCD6.
RX PubMed=11883899; DOI=10.1006/abbi.2001.2736;
RA Kitaura Y., Satoh H., Takahashi H., Shibata H., Maki M.;
RT "Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized
RT by dimerization through their fifth EF-hand regions.";
RL Arch. Biochem. Biophys. 399:12-18(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PDCD6. Dissociates from
CC PDCD6 in presence of Ca(2+).
CC -!- INTERACTION:
CC Q15038:DAZAP2; NbExp=3; IntAct=EBI-724639, EBI-724310;
CC Q53G59:KLHL12; NbExp=2; IntAct=EBI-724639, EBI-740929;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Note=Membrane-associated in the presence of Ca(2+).
CC -!- SIMILARITY: Contains 5 EF-hand domains.
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; AB026628; BAA85163.1; -; mRNA.
DR EMBL; AB018357; BAA84922.1; -; mRNA.
DR EMBL; AY359011; AAQ89370.1; -; mRNA.
DR EMBL; AK001420; BAA91680.1; -; mRNA.
DR EMBL; CR542139; CAG46936.1; -; mRNA.
DR EMBL; BC002773; AAH02773.1; -; mRNA.
DR EMBL; BC012561; AAH12561.1; -; mRNA.
DR RefSeq; NP_036524.1; NM_012392.3.
DR UniGene; Hs.470417; -.
DR ProteinModelPortal; Q9UBV8; -.
DR SMR; Q9UBV8; 123-278.
DR IntAct; Q9UBV8; 11.
DR MINT; MINT-5003645; -.
DR STRING; 9606.ENSP00000362807; -.
DR PhosphoSite; Q9UBV8; -.
DR DMDM; 74761895; -.
DR REPRODUCTION-2DPAGE; IPI00018235; -.
DR PaxDb; Q9UBV8; -.
DR PRIDE; Q9UBV8; -.
DR DNASU; 553115; -.
DR Ensembl; ENST00000373703; ENSP00000362807; ENSG00000162517.
DR GeneID; 553115; -.
DR KEGG; hsa:553115; -.
DR UCSC; uc001bth.2; human.
DR CTD; 553115; -.
DR GeneCards; GC01M032095; -.
DR HGNC; HGNC:30009; PEF1.
DR MIM; 610033; gene.
DR neXtProt; NX_Q9UBV8; -.
DR PharmGKB; PA142671184; -.
DR eggNOG; NOG249191; -.
DR HOGENOM; HOG000231983; -.
DR HOVERGEN; HBG004492; -.
DR InParanoid; Q9UBV8; -.
DR OMA; FLQGCPG; -.
DR OrthoDB; EOG7RV9FM; -.
DR PhylomeDB; Q9UBV8; -.
DR GeneWiki; PEF1; -.
DR GenomeRNAi; 553115; -.
DR NextBio; 112375; -.
DR PRO; PR:Q9UBV8; -.
DR ArrayExpress; Q9UBV8; -.
DR Bgee; Q9UBV8; -.
DR CleanEx; HS_PEF1; -.
DR Genevestigator; Q9UBV8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0051592; P:response to calcium ion; IPI:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 3.
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; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1 284 Peflin.
FT /FTId=PRO_0000247045.
FT REPEAT 21 29 1.
FT REPEAT 31 39 2.
FT REPEAT 41 49 3.
FT REPEAT 50 58 4.
FT REPEAT 59 67 5.
FT REPEAT 76 84 6.
FT REPEAT 85 92 7.
FT REPEAT 93 100 8.
FT REPEAT 101 109 9.
FT DOMAIN 114 149 EF-hand 1.
FT DOMAIN 155 183 EF-hand 2.
FT DOMAIN 181 216 EF-hand 3.
FT DOMAIN 217 253 EF-hand 4.
FT DOMAIN 254 283 EF-hand 5.
FT CA_BIND 127 138 1 (Potential).
FT CA_BIND 194 205 2 (Potential).
FT REGION 21 109 9 X 9 AA approximate tandem repeat of
FT [AP]-P-G-G-P-Y-G-G-P-P.
FT REGION 204 284 Required for interaction with PDCD6.
SQ SEQUENCE 284 AA; 30381 MW; 2E9AA5750CB7A68A CRC64;
MASYPYRQGC PGAAGQAPGA PPGSYYPGPP NSGGQYGSGL PPGGGYGGPA PGGPYGPPAG
GGPYGHPNPG MFPSGTPGGP YGGAAPGGPY GQPPPSSYGA QQPGLYGQGG APPNVDPEAY
SWFQSVDSDH SGYISMKELK QALVNCNWSS FNDETCLMMI NMFDKTKSGR IDVYGFSALW
KFIQQWKNLF QQYDRDRSGS ISYTELQQAL SQMGYNLSPQ FTQLLVSRYC PRSANPAMQL
DRFIQVCTQL QVLTEAFREK DTAVQGNIRL SFEDFVTMTA SRML
//
MIM
610033
*RECORD*
*FIELD* NO
610033
*FIELD* TI
*610033 PENTA-EF-HAND DOMAIN-CONTAINING PROTEIN 1; PEF1
;;PEFLIN
*FIELD* TX
DESCRIPTION
read more
PEF1 is a Ca(2+)-binding protein that belongs to the penta-EF-hand (PEF)
protein family, which includes the calpain small subunit (CAPNS1;
114170), sorcin (SRI; 182520), grancalcin (GCA; 607030), and ALG2
(PDCD6; 601057) (Kitaura et al., 2001).
CLONING
By searching databases for novel PEF proteins, followed by RT-PCR and
5-prime and 3-prime RACE, Kitaura et al. (1999) cloned full-length PEF1,
which they designated peflin. The deduced 284-amino acid protein has a
calculated molecular mass of 30.3 kD. PEF1 contains an N-terminal
hydrophobic domain, 5 C-terminal EF-hand motifs, and several potential
phosphorylation sites. It shares about 30% amino acid identity with
ALG2. Northern blot analysis detected a 1.8-kb PEF1 transcript in
several human cell lines. Western blot analysis showed endogenous PEF1
with an apparent molecular mass of 30 kD.
GENE FUNCTION
Kitaura et al. (2001) found that ALG2 coimmunoprecipitated with peflin
from Jurkat human T cells and from transfected HEK293 cells. Peflin
dissociated from ALG2 in the presence of Ca(2+), and the N-terminal
hydrophobic domain of peflin was not essential for heterodimerization.
Peflin and ALG2 colocalized in the cytoplasm, but ALG2 was also detected
in nuclei, as revealed by immunofluorescence staining and subcellular
fractionation. Peflin was recovered in the cytosolic fraction in the
absence of Ca(2+) and in the membrane/cytoskeletal fraction in the
presence of Ca(2+). Kitaura et al. (2001) concluded that peflin may
modulate the function of ALG2 in Ca(2+) signaling.
MAPPING
The International Radiation Mapping Consortium mapped the PEF1 gene to
chromosome 1 (TMAP RH79572).
*FIELD* RF
1. Kitaura, Y.; Matsumoto, S.; Satoh, H.; Hitomi, K.; Maki, M.: Peflin
and ALG-2, members of the penta-EF-hand protein family, form a heterodimer
that dissociates in a Ca(2+)-dependent manner. J. Biol. Chem. 276:
14053-14058, 2001.
2. Kitaura, Y.; Watanabe, M.; Satoh, H.; Kawai, T.; Hitomi, K.; Maki,
M.: Peflin, a novel member of the five-EF-hand-protein family, is
similar to the apoptosis-linked gene 2 (ALG-2) protein but possesses
nonapeptide repeats in the N-terminal hydrophobic region. Biochem.
Biophys. Res. Commun. 263: 68-75, 1999.
*FIELD* CD
Patricia A. Hartz: 4/7/2006
*FIELD* ED
terry: 05/10/2006
mgross: 4/7/2006
*RECORD*
*FIELD* NO
610033
*FIELD* TI
*610033 PENTA-EF-HAND DOMAIN-CONTAINING PROTEIN 1; PEF1
;;PEFLIN
*FIELD* TX
DESCRIPTION
read more
PEF1 is a Ca(2+)-binding protein that belongs to the penta-EF-hand (PEF)
protein family, which includes the calpain small subunit (CAPNS1;
114170), sorcin (SRI; 182520), grancalcin (GCA; 607030), and ALG2
(PDCD6; 601057) (Kitaura et al., 2001).
CLONING
By searching databases for novel PEF proteins, followed by RT-PCR and
5-prime and 3-prime RACE, Kitaura et al. (1999) cloned full-length PEF1,
which they designated peflin. The deduced 284-amino acid protein has a
calculated molecular mass of 30.3 kD. PEF1 contains an N-terminal
hydrophobic domain, 5 C-terminal EF-hand motifs, and several potential
phosphorylation sites. It shares about 30% amino acid identity with
ALG2. Northern blot analysis detected a 1.8-kb PEF1 transcript in
several human cell lines. Western blot analysis showed endogenous PEF1
with an apparent molecular mass of 30 kD.
GENE FUNCTION
Kitaura et al. (2001) found that ALG2 coimmunoprecipitated with peflin
from Jurkat human T cells and from transfected HEK293 cells. Peflin
dissociated from ALG2 in the presence of Ca(2+), and the N-terminal
hydrophobic domain of peflin was not essential for heterodimerization.
Peflin and ALG2 colocalized in the cytoplasm, but ALG2 was also detected
in nuclei, as revealed by immunofluorescence staining and subcellular
fractionation. Peflin was recovered in the cytosolic fraction in the
absence of Ca(2+) and in the membrane/cytoskeletal fraction in the
presence of Ca(2+). Kitaura et al. (2001) concluded that peflin may
modulate the function of ALG2 in Ca(2+) signaling.
MAPPING
The International Radiation Mapping Consortium mapped the PEF1 gene to
chromosome 1 (TMAP RH79572).
*FIELD* RF
1. Kitaura, Y.; Matsumoto, S.; Satoh, H.; Hitomi, K.; Maki, M.: Peflin
and ALG-2, members of the penta-EF-hand protein family, form a heterodimer
that dissociates in a Ca(2+)-dependent manner. J. Biol. Chem. 276:
14053-14058, 2001.
2. Kitaura, Y.; Watanabe, M.; Satoh, H.; Kawai, T.; Hitomi, K.; Maki,
M.: Peflin, a novel member of the five-EF-hand-protein family, is
similar to the apoptosis-linked gene 2 (ALG-2) protein but possesses
nonapeptide repeats in the N-terminal hydrophobic region. Biochem.
Biophys. Res. Commun. 263: 68-75, 1999.
*FIELD* CD
Patricia A. Hartz: 4/7/2006
*FIELD* ED
terry: 05/10/2006
mgross: 4/7/2006