ID   PAL4A_HUMAN             Reviewed;         164 AA.
AC   Q9Y536;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A-like 4A {ECO:0000305};
DE            Short=PPIase A-like 4A;
DE            EC=5.2.1.8;
DE   AltName: Full=Chromosome one-amplified sequence 2 {ECO:0000303|PubMed:11948409};
DE            Short=COAS-2 {ECO:0000303|PubMed:11948409};
DE   AltName: Full=Cyclophilin homolog overexpressed in liver cancer {ECO:0000303|Ref.1};
GN   Name=PPIAL4A {ECO:0000312|HGNC:HGNC:24369};
GN   Synonyms=COAS2 {ECO:0000312|HGNC:HGNC:24369}, PPIAL4B
GN   {ECO:0000312|HGNC:HGNC:24369};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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., Nesland J.M.,
RA   Knuutila S., Myklebost O.;
RT   "Positional cloning identifies a novel cyclophilin as a candidate amplified
RT   oncogene in 1q21.";
RL   Oncogene 21:2261-2269(2002).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62937}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, ovary and mammary gland.
CC       Moderately expressed in lung, salivary gland, kidney, skin, adipose
CC       tissue, intestine and spleen. Weakly expressed in skeletal muscle,
CC       liver and stomach. Expressed in pleiomorphic and undifferentiated
CC       liposarcomas, osteosarcomas and breast carcinomas.
CC       {ECO:0000269|PubMed:11948409}.
CC   -!- MISCELLANEOUS: It is one of six related genes or pseudogenes found in a
CC       cluster, thought to result from gene duplication, on chromosome 1.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB084917; BAB92073.1; -; mRNA.
DR   EMBL; AC253572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022240; CAB46877.1; -; Genomic_DNA.
DR   EMBL; AL451058; CAH71953.1; -; Genomic_DNA.
DR   EMBL; BX248398; CAI18814.1; -; Genomic_DNA.
DR   CCDS; CCDS76197.1; -.
DR   RefSeq; NP_001137355.1; NM_001143883.2.
DR   AlphaFoldDB; Q9Y536; -.
DR   SMR; Q9Y536; -.
DR   BioGRID; 575836; 10.
DR   IntAct; Q9Y536; 6.
DR   MINT; Q9Y536; -.
DR   STRING; 9606.ENSP00000485206; -.
DR   iPTMnet; Q9Y536; -.
DR   PhosphoSitePlus; Q9Y536; -.
DR   SwissPalm; Q9Y536; -.
DR   BioMuta; PPIAL4A; -.
DR   EPD; Q9Y536; -.
DR   jPOST; Q9Y536; -.
DR   MassIVE; Q9Y536; -.
DR   MaxQB; Q9Y536; -.
DR   PaxDb; 9606-ENSP00000485206; -.
DR   PeptideAtlas; Q9Y536; -.
DR   ProteomicsDB; 86284; -.
DR   Antibodypedia; 75827; 39 antibodies from 9 providers.
DR   DNASU; 164022; -.
DR   Ensembl; ENST00000577856.3; ENSP00000485206.1; ENSG00000263353.4.
DR   Ensembl; ENST00000709428.1; ENSP00000517691.1; ENSG00000291978.1.
DR   GeneID; 653505; -.
DR   KEGG; hsa:653505; -.
DR   MANE-Select; ENST00000577856.3; ENSP00000485206.1; NM_001143883.4; NP_001137355.1.
DR   UCSC; uc031upa.2; human.
DR   AGR; HGNC:24369; -.
DR   CTD; 653505; -.
DR   GeneCards; PPIAL4A; -.
DR   HGNC; HGNC:24369; PPIAL4A.
DR   HPA; ENSG00000263353; Not detected.
DR   MIM; 608608; gene.
DR   neXtProt; NX_Q9Y536; -.
DR   OpenTargets; ENSG00000263353; -.
DR   PharmGKB; PA164724917; -.
DR   VEuPathDB; HostDB:ENSG00000263353; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   GeneTree; ENSGT00950000183087; -.
DR   InParanoid; Q9Y536; -.
DR   OMA; ITHGNGY; -.
DR   OrthoDB; 4645060at2759; -.
DR   PhylomeDB; Q9Y536; -.
DR   TreeFam; TF316719; -.
DR   PathwayCommons; Q9Y536; -.
DR   SignaLink; Q9Y536; -.
DR   BioGRID-ORCS; 653505; 37 hits in 628 CRISPR screens.
DR   GenomeRNAi; 653505; -.
DR   Pharos; Q9Y536; Tdark.
DR   PRO; PR:Q9Y536; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9Y536; Protein.
DR   Bgee; ENSG00000263353; Expressed in primordial germ cell in gonad and 33 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF450; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A-LIKE 4A; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..164
FT                   /note="Peptidyl-prolyl cis-trans isomerase A-like 4A"
FT                   /id="PRO_0000324640"
FT   DOMAIN          7..163
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
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
//