PAL4E_HUMAN
ID PAL4E_HUMAN Reviewed; 164 AA.
AC A0A075B759;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A-like 4E {ECO:0000305};
DE Short=PPIase A-like 4E;
DE EC=5.2.1.8;
GN Name=PPIAL4E {ECO:0000312|HGNC:HGNC:33997};
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC246785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS76201.1; -.
DR RefSeq; NP_001137504.2; NM_001144032.2.
DR RefSeq; NP_001157734.2; NM_001164262.2.
DR AlphaFoldDB; A0A075B759; -.
DR SMR; A0A075B759; -.
DR STRING; 9606.ENSP00000463419; -.
DR GlyGen; A0A075B759; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A0A075B759; -.
DR PhosphoSitePlus; A0A075B759; -.
DR BioMuta; PPIAL4E; -.
DR jPOST; A0A075B759; -.
DR MassIVE; A0A075B759; -.
DR DNASU; 730262; -.
DR Ensembl; ENST00000581164.2; ENSP00000463419.1; ENSG00000271567.2.
DR GeneID; 728945; -.
DR GeneID; 730262; -.
DR KEGG; hsa:728945; -.
DR KEGG; hsa:730262; -.
DR MANE-Select; ENST00000581138.4; ENSP00000485638.1; NM_001164262.3; NP_001157734.2.
DR MANE-Select; ENST00000581164.2; ENSP00000463419.1; NM_001144032.3; NP_001137504.2.
DR UCSC; uc010paz.2; human.
DR CTD; 728945; -.
DR CTD; 730262; -.
DR GeneCards; PPIAL4E; -.
DR HGNC; HGNC:33997; PPIAL4E.
DR HPA; ENSG00000271567; Not detected.
DR neXtProt; NX_A0A075B759; -.
DR VEuPathDB; HostDB:ENSG00000271567; -.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_3_1; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; A0A075B759; -.
DR PathwayCommons; A0A075B759; -.
DR BioGRID-ORCS; 728945; 24 hits in 176 CRISPR screens.
DR BioGRID-ORCS; 730262; 20 hits in 159 CRISPR screens.
DR Pharos; A0A075B759; Tdark.
DR PRO; PR:A0A075B759; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; A0A075B759; protein.
DR Bgee; ENSG00000271567; Expressed in granulocyte and 70 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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..164
FT /note="Peptidyl-prolyl cis-trans isomerase A-like 4E"
FT /id="PRO_0000433925"
FT DOMAIN 7..163
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 164 AA; 18197 MW; FD7DF57F1A6FDAA9 CRC64;
MVNSVVFFEI TRDGKPLGRI SIKLFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF
MCQGGDFTRP NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICAAKTE
WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF
