SC65_HUMAN
ID SC65_HUMAN Reviewed; 437 AA.
AC Q92791; Q53GI6; Q9H4F6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Endoplasmic reticulum protein SC65 {ECO:0000303|PubMed:23959653};
DE AltName: Full=Leprecan-like protein 4;
DE AltName: Full=Nucleolar autoantigen No55 {ECO:0000303|PubMed:10952778, ECO:0000303|PubMed:8862517};
DE AltName: Full=Prolyl 3-hydroxylase family member 4 {ECO:0000312|HGNC:HGNC:16946};
DE AltName: Full=Synaptonemal complex protein SC65 {ECO:0000250|UniProtKB:Q64375};
DE Flags: Precursor;
GN Name=P3H4 {ECO:0000312|HGNC:HGNC:16946};
GN Synonyms=LEPREL4, NOL55, SC65 {ECO:0000250|UniProtKB:Q64375};
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Urinary bladder urothelium;
RX PubMed=8862517; DOI=10.1091/mbc.7.7.1015;
RA Ochs R.L., Stein T.W. Jr., Chan E.K.L., Ruutu M., Tan E.M.;
RT "cDNA cloning and characterization of a novel nucleolar protein.";
RL Mol. Biol. Cell 7:1015-1024(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ARG-186.
RX PubMed=10952778; DOI=10.1054/bjoc.2000.1365;
RA Fossa A., Siebert R., Aasheim H.-C., Maelandsmo G.M., Berner A.,
RA Fossa S.D., Paus E., Smeland E.B., Gaudernack G.;
RT "Identification of nucleolar protein No55 as a tumour-associated
RT autoantigen in patients with prostate cancer.";
RL Br. J. Cancer 83:743-749(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-186.
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 58-64; 122-133; 161-171; 214-221; 230-240 AND 315-337,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23959653; DOI=10.1002/jbmr.2075;
RA Gruenwald K., Castagnola P., Besio R., Dimori M., Chen Y., Akel N.S.,
RA Swain F.L., Skinner R.A., Eyre D.R., Gaddy D., Suva L.J., Morello R.;
RT "Sc65 is a novel endoplasmic reticulum protein that regulates bone mass
RT homeostasis.";
RL J. Bone Miner. Res. 29:666-675(2014).
CC -!- FUNCTION: Part of a complex composed of PLOD1, P3H3 and P3H4 that
CC catalyzes hydroxylation of lysine residues in collagen alpha chains and
CC is required for normal assembly and cross-linking of collagen fibrils.
CC Required for normal bone density and normal skin stability via its role
CC in hydroxylation of lysine residues in collagen alpha chains and in
CC collagen fibril assembly. {ECO:0000250|UniProtKB:Q8K2B0}.
CC -!- SUBUNIT: Interacts with PLOD1, P3H3 and PPIB. Identified in a complex
CC with PLOD1 and P3H3. {ECO:0000250|UniProtKB:Q8K2B0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:23959653}.
CC -!- TISSUE SPECIFICITY: Detected in fibroblasts (at protein level)
CC (PubMed:23959653). Detected in spleen, prostate, testis, ovary, colon,
CC pancreas, kidney, placenta and heart (PubMed:10952778).
CC {ECO:0000269|PubMed:10952778, ECO:0000269|PubMed:23959653}.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
CC -!- CAUTION: Was originally identified in the nucleolus (PubMed:8862517). A
CC recent publication found it only in the endoplasmic reticulum, which
CC agrees with its biological function and the predicted signal sequence
CC (PubMed:23959653). {ECO:0000269|PubMed:23959653,
CC ECO:0000269|PubMed:8862517}.
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DR EMBL; U47621; AAC51792.1; -; mRNA.
DR EMBL; AJ250583; CAC16786.1; -; mRNA.
DR EMBL; AK222945; BAD96665.1; -; mRNA.
DR EMBL; BC001047; AAH01047.1; -; mRNA.
DR EMBL; BC007942; AAH07942.1; -; mRNA.
DR EMBL; BC011701; AAH11701.1; -; mRNA.
DR CCDS; CCDS11408.1; -.
DR RefSeq; NP_006446.1; NM_006455.2.
DR AlphaFoldDB; Q92791; -.
DR SMR; Q92791; -.
DR BioGRID; 115855; 206.
DR IntAct; Q92791; 11.
DR STRING; 9606.ENSP00000347649; -.
DR GlyConnect; 1782; 2 N-Linked glycans (1 site).
DR GlyGen; Q92791; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q92791; -.
DR PhosphoSitePlus; Q92791; -.
DR BioMuta; P3H4; -.
DR DMDM; 3183090; -.
DR EPD; Q92791; -.
DR jPOST; Q92791; -.
DR MassIVE; Q92791; -.
DR MaxQB; Q92791; -.
DR PaxDb; Q92791; -.
DR PeptideAtlas; Q92791; -.
DR PRIDE; Q92791; -.
DR ProteomicsDB; 75471; -.
DR Antibodypedia; 28941; 136 antibodies from 24 providers.
DR DNASU; 10609; -.
DR Ensembl; ENST00000355468.7; ENSP00000347649.2; ENSG00000141696.13.
DR Ensembl; ENST00000393928.6; ENSP00000377505.1; ENSG00000141696.13.
DR GeneID; 10609; -.
DR KEGG; hsa:10609; -.
DR MANE-Select; ENST00000393928.6; ENSP00000377505.1; NM_006455.3; NP_006446.1.
DR UCSC; uc002hxt.4; human.
DR CTD; 10609; -.
DR DisGeNET; 10609; -.
DR GeneCards; P3H4; -.
DR HGNC; HGNC:16946; P3H4.
DR HPA; ENSG00000141696; Low tissue specificity.
DR MIM; 617419; gene.
DR neXtProt; NX_Q92791; -.
DR OpenTargets; ENSG00000141696; -.
DR VEuPathDB; HostDB:ENSG00000141696; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000153814; -.
DR HOGENOM; CLU_029887_0_0_1; -.
DR InParanoid; Q92791; -.
DR OMA; EAFCGRN; -.
DR OrthoDB; 607176at2759; -.
DR PhylomeDB; Q92791; -.
DR TreeFam; TF320837; -.
DR PathwayCommons; Q92791; -.
DR SignaLink; Q92791; -.
DR BioGRID-ORCS; 10609; 28 hits in 1073 CRISPR screens.
DR ChiTaRS; P3H4; human.
DR GeneWiki; SC65; -.
DR GenomeRNAi; 10609; -.
DR Pharos; Q92791; Tbio.
DR PRO; PR:Q92791; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92791; protein.
DR Bgee; ENSG00000141696; Expressed in stromal cell of endometrium and 151 other tissues.
DR ExpressionAtlas; Q92791; baseline and differential.
DR Genevisible; Q92791; HS.
DR GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; TAS:ProtInc.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0000795; C:synaptonemal complex; TAS:ProtInc.
DR GO; GO:0046849; P:bone remodeling; ISS:UniProtKB.
DR GO; GO:0032964; P:collagen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISS:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; TAS:ProtInc.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR033213; SC65.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13986:SF4; PTHR13986:SF4; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..437
FT /note="Endoplasmic reticulum protein SC65"
FT /evidence="ECO:0000255"
FT /id="PRO_0000150367"
FT REGION 381..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..415
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 186
FT /note="Q -> R (in dbSNP:rs13412)"
FT /evidence="ECO:0000269|PubMed:10952778, ECO:0000269|Ref.3"
FT /id="VAR_020417"
SQ SEQUENCE 437 AA; 50381 MW; 50C82FCE9BB7274A CRC64;
MARVAWGLLW LLLGSAGAQY EKYSFRGFPP EDLMPLAAAY GHALEQYEGE SWRESARYLE
AALRLHRLLR DSEAFCHANC SGPAPAAKPD PDGGRADEWA CELRLFGRVL ERAACLRRCK
RTLPAFQVPY PPRQLLRDFQ SRLPYQYLHY ALFKANRLEK AVAAAYTFLQ RNPKHELTAK
YLNYYQGMLD VADESLTDLE AQPYEAVFLR AVKLYNSGDF RSSTEDMERA LSEYLAVFAR
CLAGCEGAHE QVDFKDFYPA IADLFAESLQ CKVDCEANLT PNVGGYFVDK FVATMYHYLQ
FAYYKLNDVR QAARSAASYM LFDPKDSVMQ QNLVYYRFHR ARWGLEEEDF QPREEAMLYH
NQTAELRELL EFTHMYLQSD DEMELEETEP PLEPEDALSD AEFEGEGDYE EGMYADWWQE
PDAKGDEAEA EPEPELA
