SC61B_MOUSE
ID SC61B_MOUSE Reviewed; 96 AA.
AC Q9CQS8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein transport protein Sec61 subunit beta;
GN Name=Sec61b {ECO:0000303|PubMed:28375157, ECO:0000312|MGI:MGI:1913462};
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=C57BL/6J; TISSUE=Embryo, and Stomach;
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 STRAIN=C57BL/6J; 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 [3]
RP PROTEIN SEQUENCE OF 2-16 AND 47-57, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION.
RX PubMed=28375157; DOI=10.1172/jci90129;
RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M.,
RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E.,
RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P.,
RA Torres V.E., Somlo S.;
RT "Isolated polycystic liver disease genes define effectors of polycystin-1
RT function.";
RL J. Clin. Invest. 127:1772-1785(2017).
CC -!- FUNCTION: Component of SEC61 channel-forming translocon complex that
CC mediates transport of signal peptide-containing precursor polypeptides
CC across the endoplasmic reticulum (ER). Component of a ribosome-
CC associated ER translocon complex involved in multi-pass membrane
CC protein transport into the ER membrane and biogenesis. The SEC61
CC channel cooperates with the translocating protein TRAM1 to import
CC nascent proteins into the ER (By similarity). Required for
CC PKD1/Polycystin-1 biogenesis (PubMed:28375157).
CC {ECO:0000250|UniProtKB:P60468, ECO:0000269|PubMed:28375157}.
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 (By similarity). Interacts with TRAM1 (By
CC similarity). {ECO:0000250|UniProtKB:P60467,
CC ECO:0000250|UniProtKB:P60468}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P60468}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}.
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DR EMBL; AK004505; BAB23338.1; -; mRNA.
DR EMBL; AK008739; BAB25868.1; -; mRNA.
DR EMBL; BC002089; AAH02089.1; -; mRNA.
DR EMBL; BC081445; AAH81445.1; -; mRNA.
DR CCDS; CCDS38759.1; -.
DR RefSeq; NP_077133.1; NM_024171.2.
DR AlphaFoldDB; Q9CQS8; -.
DR SMR; Q9CQS8; -.
DR BioGRID; 211302; 7.
DR CORUM; Q9CQS8; -.
DR IntAct; Q9CQS8; 2.
DR STRING; 10090.ENSMUSP00000067681; -.
DR iPTMnet; Q9CQS8; -.
DR PhosphoSitePlus; Q9CQS8; -.
DR SwissPalm; Q9CQS8; -.
DR EPD; Q9CQS8; -.
DR jPOST; Q9CQS8; -.
DR MaxQB; Q9CQS8; -.
DR PaxDb; Q9CQS8; -.
DR PeptideAtlas; Q9CQS8; -.
DR PRIDE; Q9CQS8; -.
DR ProteomicsDB; 255349; -.
DR TopDownProteomics; Q9CQS8; -.
DR DNASU; 66212; -.
DR Ensembl; ENSMUST00000065678; ENSMUSP00000067681; ENSMUSG00000053317.
DR GeneID; 66212; -.
DR KEGG; mmu:66212; -.
DR UCSC; uc008sur.1; mouse.
DR CTD; 10952; -.
DR MGI; MGI:1913462; Sec61b.
DR VEuPathDB; HostDB:ENSMUSG00000053317; -.
DR eggNOG; KOG3457; Eukaryota.
DR GeneTree; ENSGT00960000191234; -.
DR HOGENOM; CLU_133423_4_0_1; -.
DR InParanoid; Q9CQS8; -.
DR OMA; WGKYTRG; -.
DR OrthoDB; 1634609at2759; -.
DR PhylomeDB; Q9CQS8; -.
DR TreeFam; TF313144; -.
DR BioGRID-ORCS; 66212; 9 hits in 75 CRISPR screens.
DR ChiTaRS; Sec61b; mouse.
DR PRO; PR:Q9CQS8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CQS8; protein.
DR Bgee; ENSMUSG00000053317; Expressed in parotid gland and 251 other tissues.
DR ExpressionAtlas; Q9CQS8; baseline and differential.
DR Genevisible; Q9CQS8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0048408; F:epidermal growth factor binding; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; IDA:MGI.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR InterPro; IPR030671; Sec61-beta/Sbh.
DR InterPro; IPR016482; SecG/Sec61-beta/Sbh.
DR PANTHER; PTHR13509; PTHR13509; 1.
DR Pfam; PF03911; Sec61_beta; 1.
DR PIRSF; PIRSF006398; Sec61_beta_euk; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60467,
FT ECO:0000250|UniProtKB:P60468"
FT CHAIN 2..96
FT /note="Protein transport protein Sec61 subunit beta"
FT /id="PRO_0000157255"
FT TOPO_DOM 2..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT LIPID 39
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 96 AA; 9958 MW; 5FAFF4197A742049 CRC64;
MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT
EDSPGLKVGP VPVLVMSLLF IAAVFMLHIW GKYTRS
