PRAM6_HUMAN
ID PRAM6_HUMAN Reviewed; 476 AA.
AC Q5VXH4; A0AUJ9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=PRAME family member 6 {ECO:0000305};
GN Name=PRAMEF6 {ECO:0000303|PubMed:26138980, ECO:0000312|HGNC:HGNC:30583};
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).
RN [3]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=26138980; DOI=10.1126/science.aab0515;
RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT by failed UGA/Sec decoding.";
RL Science 349:91-95(2015).
CC -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex, which mediates ubiquitination of
CC target proteins, leading to their degradation (PubMed:26138980). The
CC CRL2(PRAMEF6) complex mediates ubiquitination and degradation of
CC truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec
CC decoding (PubMed:26138980). {ECO:0000269|PubMed:26138980}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:26138980}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC PRAMEF6. {ECO:0000269|PubMed:26138980}.
CC -!- SIMILARITY: Belongs to the PRAME family. {ECO:0000305}.
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DR EMBL; AL358783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101342; AAI01343.1; -; mRNA.
DR CCDS; CCDS30594.1; -.
DR RefSeq; NP_001010889.1; NM_001010889.2.
DR AlphaFoldDB; Q5VXH4; -.
DR SMR; Q5VXH4; -.
DR STRING; 9606.ENSP00000365360; -.
DR iPTMnet; Q5VXH4; -.
DR PhosphoSitePlus; Q5VXH4; -.
DR SwissPalm; Q5VXH4; -.
DR BioMuta; PRAMEF6; -.
DR DMDM; 74757001; -.
DR MassIVE; Q5VXH4; -.
DR PaxDb; Q5VXH4; -.
DR PeptideAtlas; Q5VXH4; -.
DR PRIDE; Q5VXH4; -.
DR ProteomicsDB; 65591; -.
DR Antibodypedia; 68103; 62 antibodies from 14 providers.
DR DNASU; 440561; -.
DR Ensembl; ENST00000376189.5; ENSP00000365360.1; ENSG00000232423.6.
DR Ensembl; ENST00000415464.6; ENSP00000401281.2; ENSG00000232423.6.
DR Ensembl; ENST00000632295.1; ENSP00000487731.1; ENSG00000282119.2.
DR Ensembl; ENST00000632388.1; ENSP00000488780.1; ENSG00000282119.2.
DR GeneID; 440561; -.
DR KEGG; hsa:440561; -.
DR MANE-Select; ENST00000376189.5; ENSP00000365360.1; NM_001010889.2; NP_001010889.1.
DR UCSC; uc031tpn.1; human.
DR CTD; 440561; -.
DR GeneCards; PRAMEF6; -.
DR HGNC; HGNC:30583; PRAMEF6.
DR HPA; ENSG00000232423; Not detected.
DR neXtProt; NX_Q5VXH4; -.
DR OpenTargets; ENSG00000232423; -.
DR PharmGKB; PA142671143; -.
DR VEuPathDB; HostDB:ENSG00000232423; -.
DR eggNOG; ENOG502QWSJ; Eukaryota.
DR GeneTree; ENSGT01030000234531; -.
DR HOGENOM; CLU_039635_2_1_1; -.
DR InParanoid; Q5VXH4; -.
DR OMA; RVMMSAY; -.
DR OrthoDB; 631249at2759; -.
DR PhylomeDB; Q5VXH4; -.
DR TreeFam; TF332708; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 440561; 419 hits in 968 CRISPR screens.
DR ChiTaRS; PRAMEF6; human.
DR GenomeRNAi; 440561; -.
DR Pharos; Q5VXH4; Tdark.
DR PRO; PR:Q5VXH4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VXH4; protein.
DR Bgee; ENSG00000232423; Expressed in ectocervix.
DR Genevisible; Q5VXH4; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR026271; PRAME_family.
DR PIRSF; PIRSF038286; PRAME; 1.
PE 1: Evidence at protein level;
KW Leucine-rich repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..476
FT /note="PRAME family member 6"
FT /id="PRO_0000156980"
FT REPEAT 97..124
FT /note="LRR 1; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 179..203
FT /note="LRR 2; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 204..230
FT /note="LRR 3; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 231..266
FT /note="LRR 4; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 267..292
FT /note="LRR 5"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 293..324
FT /note="LRR 6"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 325..345
FT /note="LRR 7"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 349..376
FT /note="LRR 8"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 377..401
FT /note="LRR 9"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT CONFLICT 16
FT /note="S -> N (in Ref. 2; AAI01343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 54852 MW; 3A2FD8A09C6AC205 CRC64;
MSIRTPPRLL ELAGRSLLRD QALAMSTLEE LPTELFPPLF MEAFSRRRCE ALKLMVQAWP
FRRLPLRPLI KMPCLEAFQA VLDGLDALLT QGVHPRRWKL QVLDLQDVCE NFWMVWSEAM
ARGCFLNAKR NKTPVQDCPR MRGQQPLTVF VELWLKNRTL DEYLTCLLLW VKQRKDLLHL
CCKKLKILGM PFRNIRSILK MVNLDCIQEV EVNCKWVLPI LTQFTPYLGH MRNLQKLVLS
HMDVSRYVSP EQKKEIVTQF TTQFLKLCCL QKLSMNSVSF LEGHLDQLLS CLKTSLKVLT
ITNCVLLESD LKHLSQCPSI SQLKTLDLSG IRLTNYSLVP LQILLEKVAA TLEYLDLDDC
GIIDSQVNAI LPALSRCFEL NTFSFCGNPI SMATLENLLS HTIILKNLCV ELYPAPRESY
DADGTLCWSR FAQIRAELMK RVRDLRHPKR ILFCTDCCPD CGNRSFYDLE ADQCCC
