SEC62_MOUSE
ID SEC62_MOUSE Reviewed; 398 AA.
AC Q8BU14; Q6NX81;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Translocation protein SEC62;
DE AltName: Full=Translocation protein 1;
DE Short=TP-1;
GN Name=Sec62; Synonyms=Tloc1;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-375, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-375, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND THR-375, AND
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).
CC -!- FUNCTION: Mediates post-translational transport of precursor
CC polypeptides across endoplasmic reticulum (ER). Proposed to act as a
CC targeting receptor for small presecretory proteins containing short and
CC apolar signal peptides. Targets and properly positions newly
CC synthesized presecretory proteins into the SEC61 channel-forming
CC translocon complex, triggering channel opening for polypeptide
CC translocation to the ER lumen. {ECO:0000250|UniProtKB:Q99442}.
CC -!- SUBUNIT: The ER translocon complex that consists of channel-forming
CC core components SEC61A1, SEC61B and SEC61G and different auxiliary
CC components such as SEC62 and SEC63. Interacts with SEC61B.
CC {ECO:0000250|UniProtKB:P82009, ECO:0000250|UniProtKB:Q99442}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC62 family. {ECO:0000305}.
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DR EMBL; AK088093; BAC40140.1; -; mRNA.
DR EMBL; BC067202; AAH67202.1; -; mRNA.
DR CCDS; CCDS17286.1; -.
DR RefSeq; NP_081292.1; NM_027016.2.
DR AlphaFoldDB; Q8BU14; -.
DR SMR; Q8BU14; -.
DR BioGRID; 213329; 4.
DR STRING; 10090.ENSMUSP00000029256; -.
DR iPTMnet; Q8BU14; -.
DR PhosphoSitePlus; Q8BU14; -.
DR SwissPalm; Q8BU14; -.
DR EPD; Q8BU14; -.
DR jPOST; Q8BU14; -.
DR MaxQB; Q8BU14; -.
DR PaxDb; Q8BU14; -.
DR PeptideAtlas; Q8BU14; -.
DR PRIDE; Q8BU14; -.
DR ProteomicsDB; 256766; -.
DR Antibodypedia; 2978; 134 antibodies from 28 providers.
DR DNASU; 69276; -.
DR Ensembl; ENSMUST00000029256; ENSMUSP00000029256; ENSMUSG00000027706.
DR GeneID; 69276; -.
DR KEGG; mmu:69276; -.
DR UCSC; uc008ovh.1; mouse.
DR CTD; 7095; -.
DR MGI; MGI:1916526; Sec62.
DR VEuPathDB; HostDB:ENSMUSG00000027706; -.
DR eggNOG; KOG2927; Eukaryota.
DR GeneTree; ENSGT00390000002757; -.
DR HOGENOM; CLU_051910_0_0_1; -.
DR InParanoid; Q8BU14; -.
DR OMA; HQEQSFN; -.
DR OrthoDB; 1474000at2759; -.
DR PhylomeDB; Q8BU14; -.
DR TreeFam; TF314944; -.
DR BioGRID-ORCS; 69276; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Sec62; mouse.
DR PRO; PR:Q8BU14; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BU14; protein.
DR Bgee; ENSMUSG00000027706; Expressed in saccule of membranous labyrinth and 253 other tissues.
DR Genevisible; Q8BU14; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR InterPro; IPR004728; Sec62.
DR PANTHER; PTHR12443; PTHR12443; 1.
DR Pfam; PF03839; Sec62; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..398
FT /note="Translocation protein SEC62"
FT /id="PRO_0000206617"
FT TOPO_DOM 1..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..234
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 106..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99442"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99442"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99442"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CONFLICT 85
FT /note="L -> F (in Ref. 2; AAH67202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45581 MW; F91B3E90336FFC9F CRC64;
MAERRRHKKR IQEVGEPSKE EKAVAKYLRF NCPTKSTNMM GHRVDYFIAS KAVECLLDSK
WAKAKKGEDA LFTTRESVVD YCNRLLKKQF FHRALKVMKM KYDKDVKKEK DKGKSESGKE
DDKKSKKESV KEEKTKKEKE KKKDGEKEDS KKEETPGTPK KKETKKKFKL EPHDDQVFLD
GNEVFVWIYD PVHIKTFVMG LILVIAVIAA TLFPLWPAEM RVGVYYLSVG AGCFVASILL
LAIARCILFL IIWLITGGRH HFWFLPNLTA DVGFIDSFRP LYTHEYKGPK ADLKKDEKSE
TKKQQKSDSE EKSDSEKKED EEGKGAPADH GPEGSGGERH SDTDSDRRED DRSQHSSGNG
NDFEMITKEE LEQQTDGDCD EEDDDKDGEV PKSAHEKS
