ID   PAL4B_HUMAN             Reviewed;         164 AA.
AC   Q9Y536;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-NOV-2009, entry version 71.
DE   RecName: Full=Peptidylprolyl cis-trans isomerase A-like 4B;
DE            Short=PPIase A-like 4B;
DE            EC=5.2.1.8;
DE   AltName: Full=Chromosome 1-amplified sequence 2;
DE            Short=COAS-2;
DE   AltName: Full=Cyclophilin homolog overexpressed in liver cancer;
GN   Name=PPIAL4B; Synonyms=COAS2;
GN   and
GN   Name=PPIAL4C;
GN   and
GN   Name=PPIAL4D;
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].
RA   Tanaka S.;
RT   "Cyclophilin homologue overexpressed in liver cancer.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=11948409; DOI=10.1038/sj.onc.1205339;
RA   Meza-Zepeda L.A., Forus A., Lygren B., Dahlberg A.B., Godager L.H.,
RA   South A.P., Marenholz I., Lioumi M., Florenes V.A., Maelandsmo G.M.,
RA   Serra M., Mischke D., Nizetic D., Ragoussis J., Tarkkanen M.,
RA   Nesland J.M., Knuutila S., Myklebost O.;
RT   "Positional cloning identifies a novel cyclophilin as a candidate
RT   amplified oncogene in 1q21.";
RL   Oncogene 21:2261-2269(2002).
RN   [4]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, ovary and mammary
CC       gland. Moderately expressed in lung, salivary gland, kidney, skin,
CC       adipose tissue, intestine and spleen. Weakly expressed in skeletal
CC       muscle, liver and stomach. Expressed in pleomorphic and
CC       undifferentiated liposarcomas, osteosarcomas and breast
CC       carcinomas.
CC   -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes
CC       found in a cluster, thought to result from gene duplication, on
CC       chromosome 1.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       A subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -!- CAUTION: Expression studies do not distinguish between PPIAL4B and
CC       PPIAL4 (PubMed:11948409).
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DR   EMBL; AB084917; BAB92073.1; -; mRNA.
DR   EMBL; AL022240; CAB46877.1; -; Genomic_DNA.
DR   EMBL; AL451058; CAH71953.1; -; Genomic_DNA.
DR   EMBL; BX248398; CAI18814.1; -; Genomic_DNA.
DR   IPI; IPI00030144; -.
DR   RefSeq; NP_001129261.1; -.
DR   RefSeq; NP_001137355.1; -.
DR   RefSeq; NP_839944.1; -.
DR   UniGene; Hs.573713; -.
DR   HSSP; P52011; 1E3B.
DR   SMR; Q9Y536; 1-164.
DR   STRING; Q9Y536; -.
DR   PRIDE; Q9Y536; -.
DR   Ensembl; ENST00000369222; ENSP00000358224; ENSG00000198161; Homo sapiens.
DR   Ensembl; ENST00000369380; ENSP00000358387; ENSG00000203847; Homo sapiens.
DR   Ensembl; ENST00000436378; ENSP00000399011; ENSG00000238023; Homo sapiens.
DR   GeneID; 164022; -.
DR   GeneID; 653505; -.
DR   GeneID; 653598; -.
DR   KEGG; hsa:164022; -.
DR   KEGG; hsa:653505; -.
DR   KEGG; hsa:653598; -.
DR   UCSC; uc001ekw.1; human.
DR   CTD; 164022; -.
DR   CTD; 653505; -.
DR   CTD; 653598; -.
DR   GeneCards; GC01M143073; -.
DR   GeneCards; GC01M146419; -.
DR   GeneCards; GC01M146569; -.
DR   GeneCards; GC01P147821; -.
DR   MIM; 608608; gene.
DR   HOGENOM; Q9Y536; -.
DR   HOVERGEN; Q9Y536; -.
DR   OMA; NFAHLAN; -.
DR   BRENDA; 5.2.1.8; 247.
DR   NextBio; 88425; -.
DR   Genevestigator; Q9Y536; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; 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   Complete proteome; Cytoplasm; Isomerase; Rotamase.
FT   CHAIN         1    164       Peptidylprolyl cis-trans isomerase A-like
FT                                4B.
FT                                /FTId=PRO_0000324640.
FT   DOMAIN        7    163       PPIase cyclophilin-type.
SQ   SEQUENCE   164 AA;  18182 MW;  99D50A72B0896C4C CRC64;
     MVNSVVFFDI TVDGKPLGRI SIKLFADKIL KTAENFRALS TGEKGFRYKG SCFHRIIPGF
     MCQGGDFTRH NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICAAKTE
     WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF
//