Full text data of ZZZZ
A8K486
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Peptidyl-prolyl cis-trans isomerase; 5.2.1.8
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Peptidyl-prolyl cis-trans isomerase; 5.2.1.8
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
A8K486
ID A8K486_HUMAN Unreviewed; 165 AA.
AC A8K486;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
read moreDT 22-JAN-2014, entry version 39.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE EC=5.2.1.8;
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.
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins (By
CC similarity).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SIMILARITY: Contains PPIase cyclophilin-type domain.
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DR EMBL; AK290851; BAF83540.1; -; mRNA.
DR UniGene; Hs.356331; -.
DR ProteinModelPortal; A8K486; -.
DR SMR; A8K486; 1-165.
DR PRIDE; A8K486; -.
DR HOVERGEN; HBG001065; -.
DR NextBio; 35464097; -.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Rotamase.
SQ SEQUENCE 165 AA; 18013 MW; 9B2E637A555E4982 CRC64;
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG ETSKKITIAD CGQLE
//
ID A8K486_HUMAN Unreviewed; 165 AA.
AC A8K486;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
read moreDT 22-JAN-2014, entry version 39.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE EC=5.2.1.8;
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.
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins (By
CC similarity).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SIMILARITY: Contains PPIase cyclophilin-type domain.
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; AK290851; BAF83540.1; -; mRNA.
DR UniGene; Hs.356331; -.
DR ProteinModelPortal; A8K486; -.
DR SMR; A8K486; 1-165.
DR PRIDE; A8K486; -.
DR HOVERGEN; HBG001065; -.
DR NextBio; 35464097; -.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Rotamase.
SQ SEQUENCE 165 AA; 18013 MW; 9B2E637A555E4982 CRC64;
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG ETSKKITIAD CGQLE
//