S61A1_MOUSE
ID S61A1_MOUSE Reviewed; 476 AA.
AC P61620; P38378; P57726; Q3TXA5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein transport protein Sec61 subunit alpha isoform 1;
DE Short=Sec61 alpha-1;
GN Name=Sec61a1; Synonyms=Sec61a;
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].
RA Hayashi A., Hattori A., Okaze H., Kozuma S., Seki N., Saito T.;
RT "Mouse protein transport protein sec61 alpha subunit.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Finke K., Prehn S., Hartmann E.;
RT "Sec61 alpha isoforms.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and 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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, 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 [6]
RP FUNCTION, AND MUTAGENESIS OF VAL-67 AND THR-185.
RX PubMed=27392076; DOI=10.1016/j.ajhg.2016.05.028;
RA Bolar N.A., Golzio C., Zivna M., Hayot G., Van Hemelrijk C., Schepers D.,
RA Vandeweyer G., Hoischen A., Huyghe J.R., Raes A., Matthys E., Sys E.,
RA Azou M., Gubler M.C., Praet M., Van Camp G., McFadden K., Pediaditakis I.,
RA Pristoupilova A., Hodanova K., Vyletal P., Hartmannova H., Stranecky V.,
RA Hulkova H., Baresova V., Jedlickova I., Sovova J., Hnizda A., Kidd K.,
RA Bleyer A.J., Spong R.S., Vande Walle J., Mortier G., Brunner H.,
RA Van Laer L., Kmoch S., Katsanis N., Loeys B.L.;
RT "Heterozygous loss-of-function SEC61A1 mutations cause autosomal-dominant
RT tubulo-interstitial and glomerulocystic kidney disease with anemia.";
RL Am. J. Hum. Genet. 99:174-187(2016).
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). Forms a ribosome receptor and a
CC gated pore in the ER membrane, both functions required for
CC cotranslational translocation of nascent polypeptides. May cooperate
CC with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-
CC translational transport of small presecretory proteins. Component of a
CC ribosome-associated ER translocon complex involved in multi-pass
CC membrane protein transport into the ER membrane and biogenesis. The
CC SEC61 channel cooperates with the translocating protein TRAM1 to import
CC nascent proteins into the ER. Controls the passive efflux of calcium
CC ions from the ER lumen to the cytosol through SEC61 channel,
CC contributing to the maintenance of cellular calcium homeostasis (By
CC similarity). Plays a critical role in nephrogenesis, specifically at
CC pronephros stage (PubMed:27392076). {ECO:0000250|UniProtKB:P61619,
CC ECO:0000269|PubMed:27392076}.
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). {ECO:0000250|UniProtKB:P38377,
CC ECO:0000250|UniProtKB:P61619}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P61619}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Localizes exclusively in granular structures in the
CC endoplasmic reticulum (ER). {ECO:0000250|UniProtKB:P61619}.
CC -!- MISCELLANEOUS: When transfected in zebrafish, is able to rescue the
CC pronephric kidney tubule development phenotype of the morpholino
CC knockdown of the orthologous protein. {ECO:0000269|PubMed:27392076}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AB032902; BAA85159.1; -; mRNA.
DR EMBL; AF222743; AAG44252.1; -; mRNA.
DR EMBL; AF145253; AAF66695.1; -; mRNA.
DR EMBL; AK088473; BAC40375.1; -; mRNA.
DR EMBL; AK153055; BAE31681.1; -; mRNA.
DR EMBL; AK159349; BAE35011.1; -; mRNA.
DR EMBL; BC003707; AAH03707.1; -; mRNA.
DR CCDS; CCDS39553.1; -.
DR RefSeq; NP_058602.1; NM_016906.4.
DR AlphaFoldDB; P61620; -.
DR SMR; P61620; -.
DR BioGRID; 207315; 15.
DR CORUM; P61620; -.
DR IntAct; P61620; 2.
DR MINT; P61620; -.
DR STRING; 10090.ENSMUSP00000032168; -.
DR iPTMnet; P61620; -.
DR PhosphoSitePlus; P61620; -.
DR SwissPalm; P61620; -.
DR EPD; P61620; -.
DR jPOST; P61620; -.
DR MaxQB; P61620; -.
DR PaxDb; P61620; -.
DR PeptideAtlas; P61620; -.
DR PRIDE; P61620; -.
DR ProteomicsDB; 253386; -.
DR TopDownProteomics; P61620; -.
DR Antibodypedia; 17274; 185 antibodies from 34 providers.
DR DNASU; 53421; -.
DR Ensembl; ENSMUST00000032168; ENSMUSP00000032168; ENSMUSG00000030082.
DR GeneID; 53421; -.
DR KEGG; mmu:53421; -.
DR UCSC; uc009cvi.1; mouse.
DR CTD; 29927; -.
DR MGI; MGI:1858417; Sec61a1.
DR VEuPathDB; HostDB:ENSMUSG00000030082; -.
DR eggNOG; KOG1373; Eukaryota.
DR GeneTree; ENSGT00390000003721; -.
DR HOGENOM; CLU_031763_2_0_1; -.
DR InParanoid; P61620; -.
DR OMA; VIEDPMH; -.
DR OrthoDB; 482911at2759; -.
DR PhylomeDB; P61620; -.
DR TreeFam; TF300348; -.
DR BioGRID-ORCS; 53421; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Sec61a1; mouse.
DR PRO; PR:P61620; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P61620; protein.
DR Bgee; ENSMUSG00000030082; Expressed in internal carotid artery and 257 other tissues.
DR Genevisible; P61620; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:MGI.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; 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 GO; GO:0039019; P:pronephric nephron development; IMP:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; ISO:MGI.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.3370.10; -; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Endoplasmic reticulum; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..476
FT /note="Protein transport protein Sec61 subunit alpha
FT isoform 1"
FT /id="PRO_0000131792"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..76
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..144
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..240
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..445
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 67
FT /note="V->G: Rescued partially pronephric kidney tubule
FT atrophy in zebrafish morpholino knockdown."
FT /evidence="ECO:0000269|PubMed:27392076"
FT MUTAGEN 185
FT /note="T->A: Fails to rescue pronephric kidney tubule
FT atrophy in zebrafish morpholino knockdown."
FT /evidence="ECO:0000269|PubMed:27392076"
SQ SEQUENCE 476 AA; 52265 MW; 44A9B7B37C7C82E4 CRC64;
MAIKFLEVIK PFCVILPEIQ KPERKIQFKE KVLWTAITLF IFLVCCQIPL FGIMSSDSAD
PFYWMRVILA SNRGTLMELG ISPIVTSGLI MQLLAGAKII EVGDTPKDRA LFNGAQKLFG
MIITIGQSIV YVMTGMYGDP SEMGAGICLL ITIQLFVAGL IVLLLDELLQ KGYGLGSGIS
LFIATNICET IVWKAFSPTT VNTGRGMEFE GAIIALFHLL ATRTDKVRAL REAFYRQNLP
NLMNLIATIF VFAVVIYFQG FRVDLPIKSA RYRGQYNTYP IKLFYTSNIP IILQSALVSN
LYVISQMLSA RFSGNLLVSL LGTWSDTSSG GPARAYPVGG LCYYLSPPES FGSVLEDPVH
AVVYIVFMLG SCAFFSKTWI EVSGSSAKDV AKQLKEQQMV MRGHRETSMV HELNRYIPTA
AAFGGLCIGA LSVLADFLGA IGSGTGILLA VTIIYQYFEI FVKEQSEVGS MGALLF
