ID   FKBP2_HUMAN             Reviewed;         142 AA.
AC   P26885; Q5BJH9; Q9BTS7;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   25-JAN-2012, entry version 107.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP2;
DE            Short=PPIase FKBP2;
DE            EC=5.2.1.8;
DE   AltName: Full=13 kDa FK506-binding protein;
DE            Short=13 kDa FKBP;
DE            Short=FKBP-13;
DE   AltName: Full=FK506-binding protein 2;
DE            Short=FKBP-2;
DE   AltName: Full=Immunophilin FKBP13;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=FKBP2; Synonyms=FKBP13;
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].
RC   TISSUE=Colon carcinoma;
RX   MEDLINE=91319747; PubMed=1713687; DOI=10.1073/pnas.88.15.6677;
RA   Jin Y.-J., Albers M.W., Lane W.S., Bierer B.E., Schreiber S.L.,
RA   Burakoff S.J.;
RT   "Molecular cloning of a membrane-associated human FK506- and
RT   rapamycin-binding protein, FKBP-13.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6677-6681(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93112052; PubMed=1281998; DOI=10.1016/0006-291X(92)92276-4;
RA   Dilella A.G., Hawkins A., Craig R.J., Schreiber S.L., Griffin C.A.;
RT   "Chromosomal band assignments of the genes encoding human FKBP12 and
RT   FKBP13.";
RL   Biochem. Biophys. Res. Commun. 189:819-823(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-7.
RC   TISSUE=Placenta;
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   [4]
RP   INTERACTION WITH ARFGEF1.
RX   PubMed=12606707; DOI=10.1073/pnas.2628047100;
RA   Padilla P.I., Chang M.J., Pacheco-Rodriguez G., Adamik R., Moss J.,
RA   Vaughan M.;
RT   "Interaction of FK506-binding protein 13 with brefeldin A-inhibited
RT   guanine nucleotide-exchange protein 1 (BIG1): effects of FK506.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2322-2327(2003).
RN   [5]
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   -!- 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: Inhibited by both FK506 and rapamycin.
CC   -!- SUBUNIT: Interacts with ARFGEF1/BIG1 and the C-terminal of
CC       EPB41L2.
CC   -!- INTERACTION:
CC       Q9NRR5:UBQLN4; NbExp=2; IntAct=EBI-719873, EBI-711226;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (Probable).
CC   -!- TISSUE SPECIFICITY: T-cells and thymus.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-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; M65128; AAA58473.1; -; mRNA.
DR   EMBL; M75099; AAA36563.1; -; mRNA.
DR   EMBL; BC003384; AAH03384.1; -; mRNA.
DR   EMBL; BC091475; AAH91475.1; -; mRNA.
DR   IPI; IPI00002535; -.
DR   PIR; JC1365; JC1365.
DR   RefSeq; NP_001128680.1; NM_001135208.1.
DR   RefSeq; NP_004461.2; NM_004470.3.
DR   RefSeq; NP_476433.1; NM_057092.2.
DR   UniGene; Hs.227729; -.
DR   PDB; 2PBC; X-ray; 1.80 A; A/B/C/D=43-142.
DR   PDBsum; 2PBC; -.
DR   ProteinModelPortal; P26885; -.
DR   SMR; P26885; 43-140.
DR   IntAct; P26885; 5.
DR   MINT; MINT-1421370; -.
DR   STRING; P26885; -.
DR   DMDM; 23503054; -.
DR   OGP; P26885; -.
DR   PeptideAtlas; P26885; -.
DR   PRIDE; P26885; -.
DR   Ensembl; ENST00000309366; ENSP00000310935; ENSG00000173486.
DR   Ensembl; ENST00000394540; ENSP00000378046; ENSG00000173486.
DR   Ensembl; ENST00000449942; ENSP00000398147; ENSG00000173486.
DR   GeneID; 2286; -.
DR   KEGG; hsa:2286; -.
DR   UCSC; uc001nyy.1; human.
DR   CTD; 2286; -.
DR   GeneCards; GC11P064008; -.
DR   H-InvDB; HIX0009756; -.
DR   HGNC; HGNC:3718; FKBP2.
DR   HPA; CAB025561; -.
DR   MIM; 186946; gene.
DR   neXtProt; NX_P26885; -.
DR   PharmGKB; PA28159; -.
DR   eggNOG; prNOG15335; -.
DR   HOGENOM; HBG731200; -.
DR   HOVERGEN; HBG051623; -.
DR   InParanoid; P26885; -.
DR   OMA; DVELMKI; -.
DR   OrthoDB; EOG4Q2DGT; -.
DR   PhylomeDB; P26885; -.
DR   NextBio; 9289; -.
DR   ArrayExpress; P26885; -.
DR   Bgee; P26885; -.
DR   CleanEx; HS_FKBP2; -.
DR   Genevestigator; P26885; -.
DR   GermOnline; ENSG00000173486; Homo sapiens.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005528; F:FK506 binding; IBA:RefGenome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:RefGenome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   KO; K09569; -.
DR   PANTHER; PTHR10516; PPIase_FKBP; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Endoplasmic reticulum; Isomerase;
KW   Membrane; Polymorphism; Reference proteome; Rotamase; Signal.
FT   SIGNAL        1     21
FT   CHAIN        22    142       Peptidyl-prolyl cis-trans isomerase
FT                                FKBP2.
FT                                /FTId=PRO_0000025506.
FT   DOMAIN       49    137       PPIase FKBP-type.
FT   MOTIF       139    142       Prevents secretion from ER (Potential).
FT   VARIANT       7      7       R -> Q (in dbSNP:rs4672).
FT                                /FTId=VAR_050623.
FT   VARIANT      21     22       TA -> S.
FT                                /FTId=VAR_006410.
FT   VARIANT      25     25       A -> T.
FT                                /FTId=VAR_006411.
FT   VARIANT      97     97       C -> Y.
FT                                /FTId=VAR_006412.
FT   STRAND       51     59
FT   STRAND       65     69
FT   TURN         70     73
FT   STRAND       76     79
FT   STRAND       82     85
FT   HELIX        87     90
FT   STRAND      101    106
FT   HELIX       108    110
FT   TURN        111    115
FT   TURN        118    120
FT   STRAND      127    136
FT   HELIX       137    139
SQ   SEQUENCE   142 AA;  15649 MW;  01024F869BA7B5DA CRC64;
     MRLSWFRVLT VLSICLSAVA TATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL
     EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK
     IPGGATLVFE VELLKIERRT EL
//