PPIL6_HUMAN
ID PPIL6_HUMAN Reviewed; 311 AA.
AC Q8IXY8; A9NIU0; A9NIU9; E7EX15;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase-like 6 {ECO:0000305|PubMed:20676357};
DE Short=PPIase {ECO:0000305|PubMed:20676357};
DE AltName: Full=Cyclophilin-like protein PPIL6 {ECO:0000312|EMBL:ABC88651.1};
DE AltName: Full=Rotamase PPIL6;
GN Name=PPIL6 {ECO:0000312|HGNC:HGNC:21557};
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] (ISOFORMS 1 AND 2).
RA Chen S., Yu L.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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).
RN [5]
RP FUNCTION, AND CAUTION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
CC -!- FUNCTION: Probable inactive PPIase with no peptidyl-prolyl cis-trans
CC isomerase activity. {ECO:0000269|PubMed:20676357}.
CC -!- INTERACTION:
CC Q8IXY8; Q92624: APPBP2; NbExp=3; IntAct=EBI-12226639, EBI-743771;
CC Q8IXY8; O95429: BAG4; NbExp=3; IntAct=EBI-12226639, EBI-2949658;
CC Q8IXY8; Q86UB2: BIVM; NbExp=3; IntAct=EBI-12226639, EBI-12191873;
CC Q8IXY8; O60504: SORBS3; NbExp=3; IntAct=EBI-12226639, EBI-741237;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IXY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXY8-2; Sequence=VSP_043036;
CC Name=3;
CC IsoId=Q8IXY8-3; Sequence=VSP_055658;
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- CAUTION: Despite the fact that it belongs to the cyclophilin-type
CC PPIase family, a report has shown that it has probably no peptidyl-
CC prolyl cis-trans isomerase activity. {ECO:0000269|PubMed:20676357}.
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DR EMBL; DQ363562; ABC88651.1; -; mRNA.
DR EMBL; DQ423529; ABD83948.1; -; mRNA.
DR EMBL; AL109947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48347.1; -; Genomic_DNA.
DR EMBL; BC038716; AAH38716.1; -; mRNA.
DR CCDS; CCDS47466.2; -. [Q8IXY8-2]
DR CCDS; CCDS5074.1; -. [Q8IXY8-1]
DR CCDS; CCDS69169.1; -. [Q8IXY8-3]
DR RefSeq; NP_001104768.2; NM_001111298.2. [Q8IXY8-2]
DR RefSeq; NP_001273289.1; NM_001286360.1. [Q8IXY8-3]
DR RefSeq; NP_001273290.1; NM_001286361.1.
DR RefSeq; NP_775943.1; NM_173672.4. [Q8IXY8-1]
DR AlphaFoldDB; Q8IXY8; -.
DR SMR; Q8IXY8; -.
DR BioGRID; 130200; 6.
DR IntAct; Q8IXY8; 4.
DR STRING; 9606.ENSP00000392257; -.
DR iPTMnet; Q8IXY8; -.
DR PhosphoSitePlus; Q8IXY8; -.
DR BioMuta; PPIL6; -.
DR DMDM; 74762491; -.
DR jPOST; Q8IXY8; -.
DR MassIVE; Q8IXY8; -.
DR PeptideAtlas; Q8IXY8; -.
DR PRIDE; Q8IXY8; -.
DR ProteomicsDB; 18957; -.
DR ProteomicsDB; 71076; -. [Q8IXY8-1]
DR ProteomicsDB; 71077; -. [Q8IXY8-2]
DR Antibodypedia; 32250; 183 antibodies from 19 providers.
DR DNASU; 285755; -.
DR Ensembl; ENST00000424445.6; ENSP00000407731.2; ENSG00000185250.16. [Q8IXY8-3]
DR Ensembl; ENST00000440797.6; ENSP00000392257.2; ENSG00000185250.16. [Q8IXY8-2]
DR Ensembl; ENST00000521072.7; ENSP00000427929.1; ENSG00000185250.16. [Q8IXY8-1]
DR GeneID; 285755; -.
DR KEGG; hsa:285755; -.
DR MANE-Select; ENST00000521072.7; ENSP00000427929.1; NM_173672.5; NP_775943.1.
DR UCSC; uc003ptg.4; human. [Q8IXY8-1]
DR CTD; 285755; -.
DR DisGeNET; 285755; -.
DR GeneCards; PPIL6; -.
DR HGNC; HGNC:21557; PPIL6.
DR HPA; ENSG00000185250; Tissue enhanced (fallopian tube, testis).
DR neXtProt; NX_Q8IXY8; -.
DR OpenTargets; ENSG00000185250; -.
DR PharmGKB; PA134939571; -.
DR VEuPathDB; HostDB:ENSG00000185250; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000159634; -.
DR HOGENOM; CLU_058893_1_0_1; -.
DR InParanoid; Q8IXY8; -.
DR OMA; AFHVAKC; -.
DR OrthoDB; 1032953at2759; -.
DR PhylomeDB; Q8IXY8; -.
DR TreeFam; TF351326; -.
DR PathwayCommons; Q8IXY8; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8IXY8; -.
DR BioGRID-ORCS; 285755; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; PPIL6; human.
DR GenomeRNAi; 285755; -.
DR Pharos; Q8IXY8; Tdark.
DR PRO; PR:Q8IXY8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8IXY8; protein.
DR Bgee; ENSG00000185250; Expressed in right uterine tube and 108 other tissues.
DR ExpressionAtlas; Q8IXY8; baseline and differential.
DR Genevisible; Q8IXY8; HS.
DR GO; GO:0005737; C:cytoplasm; 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; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome.
FT CHAIN 1..311
FT /note="Probable inactive peptidyl-prolyl cis-trans
FT isomerase-like 6"
FT /id="PRO_0000263755"
FT DOMAIN 145..308
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VAR_SEQ 46..77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055658"
FT VAR_SEQ 229
FT /note="E -> EELYGSLKRSVKRQKESRGVGKIEKYR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_043036"
FT VARIANT 110
FT /note="H -> R (in dbSNP:rs9398200)"
FT /id="VAR_029620"
SQ SEQUENCE 311 AA; 35228 MW; 034E81BD5D077148 CRC64;
MARPQPCGPP HARCGSPSLP ERPLQVKVVG LFSCPNFQIA KSAAENLKNN HPSKFEDPIL
VPLQEFAWHQ YLQEKKRELK NETWEYSSSV ISFVNGQFLG DALDLQKWAH EVWDIVDIKP
SALYDALTED FSAKFLRDTK HDFVFLDICI DSSPIGRLIF ELYCDVCPKT CKNFQVLCTG
KAGFSQRGIR LHYKNSIFHR IVQNGWIQGG DIVYGKGDNG ESIYGPTFED ENFSVPHNKR
GVLGMANKGR HSNGSQFYIT LQATPYLDRK FVAFGQLIEG TEVLKQLELV PTQNERPIHM
CRITDSGDPY A
