SEC63_MOUSE
ID SEC63_MOUSE Reviewed; 760 AA.
AC Q8VHE0; E9QKG1; Q8VEB9;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Translocation protein SEC63 homolog;
GN Name=Sec63; Synonyms=Sec63l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Mack M., Noben-Trauth K.;
RT "Phenotypic characterization and positional mapping of the mouse deafness
RT mutation jackson circler (jc).";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21685914; DOI=10.1038/ng.860;
RA Fedeles S.V., Tian X., Gallagher A.R., Mitobe M., Nishio S., Lee S.H.,
RA Cai Y., Geng L., Crews C.M., Somlo S.;
RT "A genetic interaction network of five genes for human polycystic kidney
RT and liver diseases defines polycystin-1 as the central determinant of cyst
RT formation.";
RL Nat. Genet. 43:639-647(2011).
RN [6]
RP FUNCTION.
RX PubMed=22375059; DOI=10.1242/jcs.096727;
RA Lang S., Benedix J., Fedeles S.V., Schorr S., Schirra C., Schaeuble N.,
RA Jalal C., Greiner M., Hassdenteufel S., Tatzelt J., Kreutzer B.,
RA Edelmann L., Krause E., Rettig J., Somlo S., Zimmermann R., Dudek J.;
RT "Different effects of Sec61alpha, Sec62 and Sec63 depletion on transport of
RT polypeptides into the endoplasmic reticulum of mammalian cells.";
RL J. Cell Sci. 125:1958-1969(2012).
CC -!- FUNCTION: Mediates cotranslational and post-translational transport of
CC certain precursor polypeptides across endoplasmic reticulum (ER)
CC (PubMed:22375059). Proposed to play an auxiliary role in recognition of
CC precursors with short and apolar signal peptides. May cooperate with
CC SEC62 and HSPA5/BiP to facilitate targeting of small presecretory
CC proteins into the SEC61 channel-forming translocon complex, triggering
CC channel opening for polypeptide translocation to the ER lumen (By
CC similarity). Required for efficient PKD1/Polycystin-1 biogenesis and
CC trafficking to the plasma membrane of the primary cilia
CC (PubMed:21685914). {ECO:0000250|UniProtKB:Q9UGP8,
CC ECO:0000269|PubMed:21685914, ECO:0000269|PubMed:22375059}.
CC -!- SUBUNIT: The ER translocon complex consists of channel-forming core
CC components SEC61A1, SEC61B and SEC61G and different auxiliary
CC components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P82008}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:21685914}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice exhibit very early embryonic
CC lethality before E7.5. Conditional ubiquitous or kidney-specific
CC knockdown results in polycystic liver and kidney phenotypes,
CC respectively. {ECO:0000269|PubMed:21685914}.
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DR EMBL; AY024346; AAK00580.1; -; mRNA.
DR EMBL; AC124998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019366; AAH19366.1; -; mRNA.
DR EMBL; BC031846; AAH31846.1; -; mRNA.
DR CCDS; CCDS23815.1; -.
DR RefSeq; NP_694695.3; NM_153055.3.
DR AlphaFoldDB; Q8VHE0; -.
DR BioGRID; 228308; 4.
DR STRING; 10090.ENSMUSP00000019937; -.
DR iPTMnet; Q8VHE0; -.
DR PhosphoSitePlus; Q8VHE0; -.
DR SwissPalm; Q8VHE0; -.
DR EPD; Q8VHE0; -.
DR jPOST; Q8VHE0; -.
DR MaxQB; Q8VHE0; -.
DR PaxDb; Q8VHE0; -.
DR PeptideAtlas; Q8VHE0; -.
DR PRIDE; Q8VHE0; -.
DR ProteomicsDB; 256611; -.
DR Antibodypedia; 32190; 139 antibodies from 23 providers.
DR DNASU; 140740; -.
DR Ensembl; ENSMUST00000019937; ENSMUSP00000019937; ENSMUSG00000019802.
DR GeneID; 140740; -.
DR KEGG; mmu:140740; -.
DR UCSC; uc007eyx.2; mouse.
DR CTD; 11231; -.
DR MGI; MGI:2155302; Sec63.
DR VEuPathDB; HostDB:ENSMUSG00000019802; -.
DR eggNOG; KOG0721; Eukaryota.
DR GeneTree; ENSGT00390000001965; -.
DR HOGENOM; CLU_014210_1_0_1; -.
DR InParanoid; Q8VHE0; -.
DR OMA; RAILHAH; -.
DR OrthoDB; 686427at2759; -.
DR PhylomeDB; Q8VHE0; -.
DR TreeFam; TF105904; -.
DR BioGRID-ORCS; 140740; 22 hits in 75 CRISPR screens.
DR ChiTaRS; Sec63; mouse.
DR PRO; PR:Q8VHE0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VHE0; protein.
DR Bgee; ENSMUSG00000019802; Expressed in seminal vesicle and 252 other tissues.
DR Genevisible; Q8VHE0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031207; C:Sec62/Sec63 complex; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IGI:MGI.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:MGI.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:MGI.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027137; Sec63.
DR InterPro; IPR004179; Sec63-dom.
DR PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF02889; Sec63; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..760
FT /note="Translocation protein SEC63 homolog"
FT /id="PRO_0000071098"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..188
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..165
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 367..457
FT /note="SEC63 1"
FT DOMAIN 637..714
FT /note="SEC63 2"
FT REGION 492..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 603..635
FT /evidence="ECO:0000255"
FT COMPBIAS 520..535
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..760
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP8"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP8"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP8"
FT CONFLICT 48
FT /note="N -> S (in Ref. 1; AAK00580)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="R -> K (in Ref. 3; AAH19366/AAH31846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 87870 MW; 5966EDEE6F767384 CRC64;
MAGQQFQYDD SGNTFFYFLT SFVGLIVIPA TYYLWPRDQN AEQIRLKNIR KVYGRCMWYR
LRLLKPQPNI IPTVKKIVLL AGWALFLFLA YKVSKTDREY QEYNPYEVLN LDPGATVAEI
KKQYRLLSLK YHPDKGGDEV MFMRIAKAYA ALTDEESRKN WEEFGNPDGP QATSFGIALP
AWIVDQKNSI LVLLVYGLAF MVILPVVVGS WWYRSIRYSG DQILIRTTQI YTYFVYKTRN
MDMKRLIMVL AGASEFDPQY NKDSTSRPTD NILIPQLIRE IGSINLKKNE PPLTCPYSLK
ARVLLLSHLA RMKIPETLEE DQQFMLKKCP ALLQEMVNVI CQLIIMARSR EEREFRAPTL
ASLENCMKLS QMAVQGLQQF KSPLLQLPHI EEDNLRRVSN HKKYKIKTIQ DLVSLKESDR
HSLLHFLEDE KYEEVMAVLG SFPYVTMDIK SQVLDDEDSN NITVGSLVTV LVKLTRQTMA
EVFEKEQSIC AAEEQPTEDG QSDANKIKAK GGWQQKNKGP KKMPKSKKKK PLKKKPTTVP
LPQAKQQKQK QANGVVGSEA AIKEEEDDIS DKGSDSEEEE TNRDSQSEKE DGSDRESDRE
QDEKQSKDDE AEWQELQQSI QRKERALLET KSKITHPVYS LYFPEEKQEW WWLYIADRKE
QTLISMPYHV CTLKDTEEVE LKFPAPGKPG NYQYTVFLRS DSYMGLDQIK PLKLEVHEAK
PVPENHPQWD TAIEGDEDQE DSEGFEDSFE EEEEEEEGGD
