PAL4H_HUMAN
ID PAL4H_HUMAN Reviewed; 164 AA.
AC A0A075B767;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A-like 4H {ECO:0000305};
DE Short=PPIase A-like 4H;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P62937};
GN Name=PPIAL4H {ECO:0000312|HGNC:HGNC:53889};
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. {ECO:0000250|UniProtKB:P62937}.
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 Evidence={ECO:0000250|UniProtKB:P62937};
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; AC243756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011506967.1; XM_011508665.2.
DR RefSeq; XP_011508569.1; XM_011510267.2.
DR AlphaFoldDB; A0A075B767; -.
DR SMR; A0A075B767; -.
DR STRING; 9606.ENSP00000464619; -.
DR GlyGen; A0A075B767; 2 sites.
DR BioMuta; ENSG00000270339; -.
DR jPOST; A0A075B767; -.
DR MassIVE; A0A075B767; -.
DR PeptideAtlas; A0A075B767; -.
DR Antibodypedia; 74077; 3 antibodies from 2 providers.
DR Ensembl; ENST00000584068.4; ENSP00000464619.2; ENSG00000270339.4.
DR MANE-Select; ENST00000584068.4; ENSP00000464619.2; NM_001368128.3; NP_001355057.1.
DR UCSC; uc057kdh.1; human.
DR GeneCards; PPIAL4H; -.
DR HGNC; HGNC:53889; PPIAL4H.
DR HPA; ENSG00000270339; Tissue enhanced (brain).
DR neXtProt; NX_A0A075B767; -.
DR VEuPathDB; HostDB:ENSG00000270339; -.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00950000183087; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; A0A075B767; -.
DR BioGRID-ORCS; 105371242; 2 hits in 3 CRISPR screens.
DR Pharos; A0A075B767; Tdark.
DR PRO; PR:A0A075B767; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; A0A075B767; protein.
DR Bgee; ENSG00000270339; Expressed in granulocyte and 58 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; Glycoprotein; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..164
FT /note="Peptidyl-prolyl cis-trans isomerase A-like 4H"
FT /id="PRO_0000445737"
FT DOMAIN 7..163
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 164 AA; 18208 MW; E52068C3FBEE2057 CRC64;
MVNSVVFFDI TVDGKPLGRI SIKLFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF
MCQGGDFTRP NGTDDKSIYG EKFDDENLIR KHTGSGILSM VNAGPNTNGS QLFICTAKTE
WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF
