ID PPIB_HUMAN Reviewed; 216 AA. AC P23284; A8K534; Q6IBH5; Q9BVK5; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 25-NOV-2008, entry version 91. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B; DE Short=PPIase; DE Short=Rotamase; DE EC=5.2.1.8; DE AltName: Full=Cyclophilin B; DE AltName: Full=S-cyclophilin; DE Short=SCYLP; DE AltName: Full=CYP-S1; DE Flags: Precursor; GN Name=PPIB; Synonyms=CYPB; 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 MEDLINE=91250363; PubMed=2040592; RA Spik G., Haendler B., Delmas O., Mariller C., Chamoux M., Maes P., RA Tartar A., Montreuil J., Stedman K., Kocher H.P., Keller R., RA Hiestand P.C., Movva N.R.; RT "A novel secreted cyclophilin-like protein (SCYLP)."; RL J. Biol. Chem. 266:10735-10738(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Livingston R.J., Rieder M.J., Rajkumar N., Downing T.K., Olson A.N., RA Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., RA Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., RA Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., RA Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., RA Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., RA Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., RA Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., RA Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., RA Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human RT chromosome 15."; RL Nature 440:671-675(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-216, AND PROTEIN SEQUENCE OF 34-48. RX MEDLINE=91156714; PubMed=2000394; RA Price E.R., Zydowsky L.D., Jin M., Hunter C.H., McKeon F.D., RA Walsh C.T.; RT "Human cyclophilin B: a second cyclophilin gene encodes a peptidyl- RT prolyl isomerase with a signal sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 88:1903-1907(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-216. RX MEDLINE=91260697; PubMed=1710767; RA Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.; RT "An endoplasmic reticulum-specific cyclophilin."; RL Mol. Cell. Biol. 11:3484-3491(1991). RN [10] RP PROTEIN SEQUENCE OF 72-84 AND 159-165. RX MEDLINE=93162043; PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [11] RP SUBCELLULAR LOCATION. RX MEDLINE=92112948; PubMed=1530944; DOI=10.1083/jcb.116.1.113; RA Arber S., Krause K.-H., Caroni P.; RT "S-cyclophilin is retained intracellularly via a unique COOH-terminal RT sequence and colocalizes with the calcium storage protein RT calreticulin."; RL J. Cell Biol. 116:113-125(1992). RN [12] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216. RX MEDLINE=94255495; PubMed=8197205; RA Mikol V., Kallen J., Walkinshaw M.D.; RT "X-ray structure of a cyclophilin B/cyclosporin complex: comparison RT with cyclophilin A and delineation of its calcineurin-binding RT domain."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5183-5186(1994). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Cyclosporin A (CsA) inhibits CYPB. CC -!- INTERACTION: CC Q9HC24:TMBIM4; NbExp=1; IntAct=EBI-359252, EBI-1045545; CC P40337:VHL; NbExp=1; IntAct=EBI-359252, EBI-301246; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome. CC Note=Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase CC B subfamily. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator. 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; M63573; AAA36601.1; -; mRNA. DR EMBL; AY962310; AAX44050.1; -; Genomic_DNA. DR EMBL; AK291149; BAF83838.1; -; mRNA. DR EMBL; CR456829; CAG33110.1; -; mRNA. DR EMBL; AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471082; EAW77669.1; -; Genomic_DNA. DR EMBL; BC001125; AAH01125.1; -; mRNA. DR EMBL; BC008848; AAH08848.1; -; mRNA. DR EMBL; BC020800; AAH20800.1; -; mRNA. DR EMBL; BC032138; AAH32138.1; -; mRNA. DR EMBL; M60857; AAA52150.1; ALT_INIT; mRNA. DR EMBL; M60457; AAA35733.1; -; mRNA. DR PIR; A39118; CSHUB. DR RefSeq; NP_000933.1; -. DR UniGene; Hs.434937; -. DR PDB; 1CYN; X-ray; 1.85 A; A=38-216. DR PDBsum; 1CYN; -. DR IntAct; P23284; -. DR PhosphoSite; P23284; -. DR SWISS-2DPAGE; P23284; -. DR Aarhus/Ghent-2DPAGE; 117; NEPHGE. DR OGP; P23284; -. DR REPRODUCTION-2DPAGE; IPI00646304; -. DR Ensembl; ENSG00000166794; Homo sapiens. DR GeneID; 5479; -. DR KEGG; hsa:5479; -. DR H-InvDB; HIX0012337; -. DR HGNC; HGNC:9255; PPIB. DR HPA; CAB011487; -. DR HPA; HPA012720; -. DR MIM; 123841; gene. DR PharmGKB; PA33580; -. DR HOVERGEN; P23284; -. DR DrugBank; DB00172; L-Proline. DR LinkHub; P23284; -. DR NextBio; 21210; -. DR CleanEx; HS_PPIB; -. DR GermOnline; ENSG00000166794; Homo sapiens. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0005788; C:endoplasmic reticulum lumen; NAS:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; NAS:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW. DR InterPro; IPR002130; PPIase_cyclophilin. DR Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1. DR PANTHER; PTHR11071; PPIase_cyclophilin; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cyclosporin; Direct protein sequencing; KW Endoplasmic reticulum; Glycoprotein; Isomerase; Polymorphism; KW Rotamase; Signal. FT SIGNAL 1 33 FT CHAIN 34 216 Peptidyl-prolyl cis-trans isomerase B. FT /FTId=PRO_0000025479. FT DOMAIN 47 204 PPIase cyclophilin-type. FT MOTIF 213 216 Prevents secretion from ER. FT CARBOHYD 148 148 N-linked (GlcNAc...) (Potential). FT VARIANT 60 60 V -> L (in dbSNP:rs11558595). FT /FTId=VAR_047711. FT CONFLICT 5 5 S -> R (in Ref. 8; AAA52150). FT CONFLICT 216 216 E -> D (in Ref. 4; CAG33110). FT STRAND 41 52 FT STRAND 55 64 FT TURN 66 68 FT HELIX 70 81 FT TURN 82 84 FT STRAND 92 97 FT TURN 98 100 FT STRAND 101 104 FT TURN 107 109 FT STRAND 110 113 FT STRAND 137 140 FT STRAND 152 157 FT HELIX 160 162 FT TURN 163 165 FT STRAND 168 174 FT HELIX 176 183 FT STRAND 193 195 FT STRAND 197 212 SQ SEQUENCE 216 AA; 23743 MW; 2D0410A07AA9E420 CRC64; MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDVGRV IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVESTKTDSR DKPLKDVIIA DCGKIEVEKP FAIAKE //