PAL4G_HUMAN
ID PAL4G_HUMAN Reviewed; 164 AA.
AC P0DN37; A1L431; A2BFH1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A-like 4G {ECO:0000305};
DE Short=PPIase A-like 4G;
DE EC=5.2.1.8;
DE AltName: Full=Peptidylprolyl cis-trans isomerase A-like 4;
GN Name=PPIAL4G;
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}.
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DR EMBL; BX284650; CAM26887.1; -; Genomic_DNA.
DR CCDS; CCDS41375.2; -.
DR RefSeq; NP_001116540.1; NM_001123068.1.
DR AlphaFoldDB; P0DN37; -.
DR SMR; P0DN37; -.
DR IntAct; P0DN37; 18.
DR STRING; 9606.ENSP00000393845; -.
DR iPTMnet; P0DN37; -.
DR PhosphoSitePlus; P0DN37; -.
DR BioMuta; PPIAL4G; -.
DR jPOST; P0DN37; -.
DR MassIVE; P0DN37; -.
DR MaxQB; P0DN37; -.
DR PaxDb; P0DN37; -.
DR PeptideAtlas; P0DN37; -.
DR PRIDE; P0DN37; -.
DR Antibodypedia; 67885; 77 antibodies from 12 providers.
DR DNASU; 644591; -.
DR Ensembl; ENST00000419275.3; ENSP00000393845.1; ENSG00000236334.3.
DR GeneID; 644591; -.
DR KEGG; hsa:644591; -.
DR MANE-Select; ENST00000419275.3; ENSP00000393845.1; NM_001123068.3; NP_001116540.1.
DR CTD; 644591; -.
DR GeneCards; PPIAL4G; -.
DR HGNC; HGNC:33996; PPIAL4G.
DR HPA; ENSG00000236334; Tissue enhanced (brain).
DR neXtProt; NX_P0DN37; -.
DR OpenTargets; ENSG00000236334; -.
DR VEuPathDB; HostDB:ENSG00000236334; -.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00950000183087; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P0DN37; -.
DR PathwayCommons; P0DN37; -.
DR SignaLink; P0DN37; -.
DR BioGRID-ORCS; 644591; 249 hits in 980 CRISPR screens.
DR GenomeRNAi; 644591; -.
DR Pharos; P0DN37; Tdark.
DR PRO; PR:P0DN37; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P0DN37; protein.
DR Bgee; ENSG00000236334; Expressed in calcaneal tendon and 89 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 4G"
FT /id="PRO_0000324639"
FT DOMAIN 7..163
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 164 AA; 18166 MW; CEAFE5FE3D858213 CRC64;
MVNSVIFFDI TVDGKPLGRI SIKQFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF
MCQGGDFTHP NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF
