ID   PAL4C_HUMAN             Reviewed;         164 AA.
AC   A0A0B4J2A2; A1L431; A2BFH1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A-like 4C {ECO:0000305};
DE            Short=PPIase A-like 4C;
DE            EC=5.2.1.8;
GN   Name=PPIAL4C {ECO:0000312|HGNC:HGNC:33995};
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- 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; AC242842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC130376; AAI30377.1; -; mRNA.
DR   EMBL; BC130378; AAI30379.1; -; mRNA.
DR   CCDS; CCDS72898.1; -.
DR   RefSeq; NP_001129261.2; NM_001135789.3.
DR   AlphaFoldDB; A0A0B4J2A2; -.
DR   SMR; A0A0B4J2A2; -.
DR   IntAct; A0A0B4J2A2; 2.
DR   STRING; 9606.ENSP00000463057; -.
DR   iPTMnet; A0A0B4J2A2; -.
DR   PhosphoSitePlus; A0A0B4J2A2; -.
DR   BioMuta; PPIAL4C; -.
DR   jPOST; A0A0B4J2A2; -.
DR   MassIVE; A0A0B4J2A2; -.
DR   PeptideAtlas; A0A0B4J2A2; -.
DR   Antibodypedia; 77049; 9 antibodies from 4 providers.
DR   DNASU; 653598; -.
DR   Ensembl; ENST00000585245.3; ENSP00000463057.2; ENSG00000288867.1.
DR   GeneID; 653598; -.
DR   KEGG; hsa:653598; -.
DR   MANE-Select; ENST00000585245.3; ENSP00000463057.2; NM_001135789.5; NP_001129261.2.
DR   CTD; 653598; -.
DR   GeneCards; PPIAL4C; -.
DR   HGNC; HGNC:33995; PPIAL4C.
DR   HPA; ENSG00000263464; Tissue enhanced (intestine, lymphoid tissue).
DR   neXtProt; NX_A0A0B4J2A2; -.
DR   VEuPathDB; HostDB:ENSG00000263464; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   GeneTree; ENSGT00950000183087; -.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   OMA; ICSAKSE; -.
DR   OrthoDB; 1403619at2759; -.
DR   PhylomeDB; A0A0B4J2A2; -.
DR   PathwayCommons; A0A0B4J2A2; -.
DR   SignaLink; A0A0B4J2A2; -.
DR   BioGRID-ORCS; 653598; 21 hits in 238 CRISPR screens.
DR   GenomeRNAi; 653598; -.
DR   Pharos; A0A0B4J2A2; Tdark.
DR   PRO; PR:A0A0B4J2A2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; A0A0B4J2A2; protein.
DR   Bgee; ENSG00000263464; Expressed in duodenum and 64 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR   Gene3D; 2.40.100.10; -; 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   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   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..164
FT                   /note="Peptidyl-prolyl cis-trans isomerase A-like 4C"
FT                   /id="PRO_0000433924"
FT   DOMAIN          7..163
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   164 AA;  18156 MW;  8FE074FFE5657EF8 CRC64;
     MVNSVVFFDI TVDGKPLGRI SIKLFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF
     MCQGGDFTRP NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICTAKTE
     WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF