SC61G_HUMAN
ID SC61G_HUMAN Reviewed; 68 AA.
AC P60059; B2R4J0; P38384; Q6IB25;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein transport protein Sec61 subunit gamma;
GN Name=SEC61G;
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 MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP INTERACTION WITH ZIKA VIRUS FRENCH POLYNESIA 10087PF/2013 NS4A; ZIKA VIRUS
RP MR-766 NS4A AND DENGUE VIRUS DENV2 16681 NS4A.
RX PubMed=30550790; DOI=10.1016/j.cell.2018.11.028;
RA Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L.,
RA Johnson J.R., Von Dollen J., Ramage H.R., Satkamp L., Newton B.,
RA Huettenhain R., Petit M.J., Baum T., Everitt A., Laufman O., Tassetto M.,
RA Shales M., Stevenson E., Iglesias G.N., Shokat L., Tripathi S.,
RA Balasubramaniam V., Webb L.G., Aguirre S., Willsey A.J., Garcia-Sastre A.,
RA Pollard K.S., Cherry S., Gamarnik A.V., Marazzi I., Taunton J.,
RA Fernandez-Sesma A., Bellen H.J., Andino R., Krogan N.J.;
RT "Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms
RT of Dengue and Zika Virus Pathogenesis.";
RL Cell 175:1931-1945(2018).
RN [11]
RP FUNCTION, AND INTERACTION WITH TMCO1; CCDC47; NCLN; NOMO; TMEM147; SEC61A1
RP AND SEC61B.
RX PubMed=32820719; DOI=10.7554/elife.56889;
RA McGilvray P.T., Anghel S.A., Sundaram A., Zhong F., Trnka M.J.,
RA Fuller J.R., Hu H., Burlingame A.L., Keenan R.J.;
RT "An ER translocon for multi-pass membrane protein biogenesis.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Component of SEC61 channel-forming translocon complex that
CC mediates transport of signal peptide-containing precursor polypeptides
CC across endoplasmic reticulum (ER) (By similarity). Component of a
CC ribosome-associated ER translocon complex involved in multi-pass
CC membrane protein transport into the ER membrane and biogenesis
CC (PubMed:32820719). The SEC61 channel cooperates with the translocating
CC protein TRAM1 to import nascent proteins into the ER (By similarity).
CC {ECO:0000250|UniProtKB:P60058, ECO:0000250|UniProtKB:P61619,
CC ECO:0000269|PubMed:32820719}.
CC -!- SUBUNIT: The SEC61 channel-forming translocon complex consists of
CC channel-forming core components SEC61A1, SEC61B and SEC61G and
CC different auxiliary components such as SEC62 and SEC63 (By similarity).
CC The ribosome-associated ER translocon complex includes SEC61A1, SEC61B,
CC SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence
CC of ribosomes, only the complex forms with NCLN/Nicalin, NOMO and
CC TMEM147 remains intact (PubMed:32820719).
CC {ECO:0000250|UniProtKB:P60058, ECO:0000269|PubMed:32820719}.
CC -!- SUBUNIT: (Microbial infection) May interact with Zika virus strain Mr-
CC 766 non-structural protein 4A/NS4A (PubMed:30550790). May interact with
CC Zika virus French Polynesia 10087PF/2013 non-structural protein 4A/NS4A
CC (PubMed:30550790). {ECO:0000269|PubMed:30550790}.
CC -!- SUBUNIT: (Microbial infection) May interact with Dengue virus DENV2
CC 16681 non-structural protein 4A/NS4A. {ECO:0000269|PubMed:30550790}.
CC -!- INTERACTION:
CC P60059; Q13520: AQP6; NbExp=3; IntAct=EBI-4402709, EBI-13059134;
CC P60059; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-4402709, EBI-6942903;
CC P60059; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-4402709, EBI-18304435;
CC P60059; P80188: LCN2; NbExp=3; IntAct=EBI-4402709, EBI-11911016;
CC P60059; Q8N386: LRRC25; NbExp=3; IntAct=EBI-4402709, EBI-11304917;
CC P60059; O00623: PEX12; NbExp=3; IntAct=EBI-4402709, EBI-594836;
CC P60059; P11686: SFTPC; NbExp=3; IntAct=EBI-4402709, EBI-10197617;
CC P60059; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-4402709, EBI-726044;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P60058}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000305}.
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DR EMBL; AF054184; AAC99401.1; -; mRNA.
DR EMBL; CR456979; CAG33260.1; -; mRNA.
DR EMBL; AK311845; BAG34787.1; -; mRNA.
DR EMBL; CH471201; EAW50960.1; -; Genomic_DNA.
DR EMBL; BC009480; AAH09480.1; -; mRNA.
DR EMBL; BC051840; AAH51840.1; -; mRNA.
DR CCDS; CCDS5513.1; -.
DR PIR; S42412; S42412.
DR RefSeq; NP_001012474.1; NM_001012456.1.
DR RefSeq; NP_055117.1; NM_014302.3.
DR PDB; 6W6L; EM; 3.84 A; 2=1-68.
DR PDBsum; 6W6L; -.
DR AlphaFoldDB; P60059; -.
DR SMR; P60059; -.
DR BioGRID; 117039; 18.
DR IntAct; P60059; 11.
DR MINT; P60059; -.
DR STRING; 9606.ENSP00000388337; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR iPTMnet; P60059; -.
DR PhosphoSitePlus; P60059; -.
DR SwissPalm; P60059; -.
DR BioMuta; SEC61G; -.
DR DMDM; 38503386; -.
DR EPD; P60059; -.
DR jPOST; P60059; -.
DR MassIVE; P60059; -.
DR MaxQB; P60059; -.
DR PaxDb; P60059; -.
DR PeptideAtlas; P60059; -.
DR PRIDE; P60059; -.
DR ProteomicsDB; 57183; -.
DR TopDownProteomics; P60059; -.
DR Antibodypedia; 44752; 73 antibodies from 18 providers.
DR DNASU; 23480; -.
DR Ensembl; ENST00000352861.9; ENSP00000341538.4; ENSG00000132432.14.
DR Ensembl; ENST00000395535.7; ENSP00000378906.3; ENSG00000132432.14.
DR Ensembl; ENST00000415949.5; ENSP00000388337.1; ENSG00000132432.14.
DR Ensembl; ENST00000450622.1; ENSP00000409884.1; ENSG00000132432.14.
DR GeneID; 23480; -.
DR KEGG; hsa:23480; -.
DR MANE-Select; ENST00000352861.9; ENSP00000341538.4; NM_014302.4; NP_055117.1.
DR UCSC; uc003tqf.4; human.
DR CTD; 23480; -.
DR DisGeNET; 23480; -.
DR GeneCards; SEC61G; -.
DR HGNC; HGNC:18277; SEC61G.
DR HPA; ENSG00000132432; Low tissue specificity.
DR MIM; 609215; gene.
DR neXtProt; NX_P60059; -.
DR OpenTargets; ENSG00000132432; -.
DR PharmGKB; PA134939045; -.
DR VEuPathDB; HostDB:ENSG00000132432; -.
DR eggNOG; KOG3498; Eukaryota.
DR GeneTree; ENSGT00390000001319; -.
DR HOGENOM; CLU_167752_2_0_1; -.
DR InParanoid; P60059; -.
DR OMA; RDGNQFL; -.
DR OrthoDB; 1623399at2759; -.
DR PhylomeDB; P60059; -.
DR TreeFam; TF300232; -.
DR PathwayCommons; P60059; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; P60059; -.
DR SIGNOR; P60059; -.
DR BioGRID-ORCS; 23480; 703 hits in 1046 CRISPR screens.
DR ChiTaRS; SEC61G; human.
DR GeneWiki; SEC61G; -.
DR GenomeRNAi; 23480; -.
DR Pharos; P60059; Tbio.
DR PRO; PR:P60059; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P60059; protein.
DR Bgee; ENSG00000132432; Expressed in pituitary gland and 213 other tissues.
DR ExpressionAtlas; P60059; baseline and differential.
DR Genevisible; P60059; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0071261; C:Ssh1 translocon complex; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; ISS:UniProtKB.
DR Gene3D; 1.20.5.820; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR023391; Prot_translocase_SecE_dom_sf.
DR InterPro; IPR008158; Translocase_Sec61-g.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR Pfam; PF00584; SecE; 1.
DR SUPFAM; SSF103456; SSF103456; 1.
DR TIGRFAMs; TIGR00327; secE_euk_arch; 1.
DR PROSITE; PS01067; SECE_SEC61G; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..68
FT /note="Protein transport protein Sec61 subunit gamma"
FT /id="PRO_0000104195"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 68 AA; 7741 MW; 14C8279A22548561 CRC64;
MDQVMQFVEP SRQFVKDSIR LVKRCTKPDR KEFQKIAMAT AIGFAIMGFI GFFVKLIHIP
INNIIVGG
