ID   SC65_RAT                Reviewed;         443 AA.
AC   Q64375; A0A096MJK4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Endoplasmic reticulum protein SC65 {ECO:0000250|UniProtKB:Q92791};
DE   AltName: Full=Leprecan-like protein 4;
DE   AltName: Full=Prolyl 3-hydroxylase family member 4 {ECO:0000312|RGD:620767};
DE   AltName: Full=Synaptonemal complex protein SC65 {ECO:0000303|PubMed:1363622};
DE   Flags: Precursor;
GN   Name=P3h4 {ECO:0000312|RGD:620767};
GN   Synonyms=Leprel4, Sc65 {ECO:0000303|PubMed:1363622};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 30-414, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=1363622; DOI=10.1139/o92-147;
RA   Chen Q., Pearlman R.E., Moens P.B.;
RT   "Isolation and characterization of a cDNA encoding a synaptonemal complex
RT   protein.";
RL   Biochem. Cell Biol. 70:1030-1038(1992).
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:0000250|UniProtKB:Q92791}.
CC   -!- TISSUE SPECIFICITY: Found in testis, brain, heart and at a much lower
CC       level in liver. {ECO:0000269|PubMed:1363622}.
CC   -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
CC   -!- CAUTION: Was initially identified in the synaptonemal complex
CC       (PubMed:1363622). Characterization data from human and mouse indicate
CC       the protein is in the endoplasmic reticulum, which agrees with its
CC       biological function and the predicted signal sequence.
CC       {ECO:0000269|PubMed:1363622, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA46449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA46449.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AABR07072182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473948; EDM06035.1; -; Genomic_DNA.
DR   EMBL; X65454; CAA46449.1; ALT_SEQ; mRNA.
DR   PIR; A56822; A56822.
DR   RefSeq; NP_067592.2; NM_021581.2.
DR   AlphaFoldDB; Q64375; -.
DR   BioGRID; 248724; 1.
DR   IntAct; Q64375; 1.
DR   STRING; 10116.ENSRNOP00000068162; -.
DR   GlyGen; Q64375; 1 site.
DR   jPOST; Q64375; -.
DR   PaxDb; Q64375; -.
DR   Ensembl; ENSRNOT00000076585; ENSRNOP00000068162; ENSRNOG00000015787.
DR   GeneID; 59101; -.
DR   KEGG; rno:59101; -.
DR   UCSC; RGD:620767; rat.
DR   CTD; 10609; -.
DR   RGD; 620767; P3h4.
DR   eggNOG; KOG4459; Eukaryota.
DR   GeneTree; ENSGT00940000153814; -.
DR   InParanoid; Q64375; -.
DR   OMA; EAFCGRN; -.
DR   OrthoDB; 607176at2759; -.
DR   PRO; PR:Q64375; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Proteomes; UP000234681; Chromosome 10.
DR   Bgee; ENSRNOG00000015787; Expressed in ovary and 20 other tissues.
DR   ExpressionAtlas; Q64375; baseline and differential.
DR   GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0000795; C:synaptonemal complex; IDA:RGD.
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   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR033213; SC65.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR13986:SF4; PTHR13986:SF4; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..443
FT                   /note="Endoplasmic reticulum protein SC65"
FT                   /id="PRO_0000150368"
FT   REGION          81..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..443
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   443 AA;  51104 MW;  8AF13EB91B230DED CRC64;
     MARAAWGLLW LLLGSAGAQY EKYSFRGFPP EDLMPLATAY GHALEQYEGE SWRESARYLE
     AALRLHRLLR DSEAFCHANC SGPATSQPRP APGPDGDNEG DGEDWARELR LFGHVLERAA
     CLRRCKRTLP AFQVPYPSRQ LLRDFQNRLP YQYLHYAHFK ANRLEKAVAA AYTFLQRNPK
     HELTAKYLNY YRGMLDIGDE SLTDLEAQPY EAVFLQAVKL YNSGDFRSST EHMERALADY
     MTVFARCLAG CEGAHEQVDF KDFYPAIADL FAESLQCKVD CEANLTPNVG GFFVDKFVAT
     MYHYLQFAYY KLNDVHQAAR SAASYMLFDP KDSVMQQNLV YYRFHRARWG LEEEDFQPRE
     EAVLYHNQTS ELRELLDFTH MYLQSDDEME LEETESLPEP EKPLSDAEFE GEGDYEEGLY
     ADWWQEPDAK GDEDEAEPEP ELA