SSRA_HUMAN
ID SSRA_HUMAN Reviewed; 286 AA.
AC P43307; A8K685; Q53GX2; Q53H19; Q5TAM3; Q6IB43; Q8NBH9; Q96IA2; Q9TNQ8;
AC Q9UN49;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Translocon-associated protein subunit alpha;
DE Short=TRAP-alpha;
DE AltName: Full=Signal sequence receptor subunit alpha;
DE Short=SSR-alpha;
DE Flags: Precursor;
GN Name=SSR1; Synonyms=TRAPA; ORFNames=PSEC0262;
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 [MRNA] (ISOFORM 1), AND VARIANT SER-28.
RX PubMed=8050590; DOI=10.1016/0014-5793(94)00693-8;
RA Hartmann E., Prehn S.;
RT "The N-terminal region of the alpha-subunit of the TRAP complex has a
RT conserved cluster of negative charges.";
RL FEBS Lett. 349:324-326(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10437777; DOI=10.1016/s0014-5793(99)00885-6;
RA Hirama T., Miller C.W., Koeffler H.P.;
RT "Translocon-associated protein alpha transcripts are induced by
RT granulocyte-macrophage colony-stimulating factor and exhibit complex
RT alternative polyadenylation.";
RL FEBS Lett. 455:223-227(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-28.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
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 [10]
RP PROTEIN SEQUENCE OF 19-31.
RX PubMed=1557127; DOI=10.1038/356443a0;
RA Wei M.L., Cresswell P.;
RT "HLA-A2 molecules in an antigen-processing mutant cell contain signal
RT sequence-derived peptides.";
RL Nature 356:443-446(1992).
RN [11]
RP GLYCOSYLATION AT ASN-136.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-268, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-191.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260 AND SER-268, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH CALNEXIN.
RX PubMed=22314232; DOI=10.1038/emboj.2012.15;
RA Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A.,
RA Dal Peraro M., van der Goot F.G.;
RT "Palmitoylated calnexin is a key component of the ribosome-translocon
RT complex.";
RL EMBO J. 31:1823-1835(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to bind
CC calcium to the ER membrane and thereby regulate the retention of ER
CC resident proteins. May be involved in the recycling of the
CC translocation apparatus after completion of the translocation process
CC or may function as a membrane-bound chaperone facilitating folding of
CC translocated proteins.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-
CC gamma. Interacts with palmitoylated calnexin (CALX), the interaction is
CC required for efficient folding of glycosylated proteins.
CC {ECO:0000269|PubMed:22314232}.
CC -!- INTERACTION:
CC P43307; P27824: CANX; NbExp=6; IntAct=EBI-714168, EBI-355947;
CC P43307; P01009: SERPINA1; NbExp=4; IntAct=EBI-714168, EBI-986224;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43307-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43307-2; Sequence=VSP_013621;
CC -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
CC being highly negatively charged, and the cytoplasmic C-terminus
CC positively charged.
CC -!- MISCELLANEOUS: Seems to bind calcium.
CC -!- SIMILARITY: Belongs to the TRAP-alpha family. {ECO:0000305}.
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DR EMBL; Z12830; CAA78290.1; -; mRNA.
DR EMBL; AF156965; AAD48778.1; -; mRNA.
DR EMBL; BT007387; AAP36051.1; -; mRNA.
DR EMBL; AK291550; BAF84239.1; -; mRNA.
DR EMBL; CR456961; CAG33242.1; -; mRNA.
DR EMBL; AK222762; BAD96482.1; -; mRNA.
DR EMBL; AK222809; BAD96529.1; -; mRNA.
DR EMBL; AK075562; BAC11701.1; -; mRNA.
DR EMBL; AL139095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007710; AAH07710.1; -; mRNA.
DR CCDS; CCDS4499.1; -. [P43307-1]
DR PIR; I38246; I38246.
DR RefSeq; NP_001278937.1; NM_001292008.1.
DR RefSeq; NP_003135.2; NM_003144.4. [P43307-1]
DR AlphaFoldDB; P43307; -.
DR BioGRID; 112623; 405.
DR IntAct; P43307; 72.
DR MINT; P43307; -.
DR STRING; 9606.ENSP00000244763; -.
DR GlyConnect; 1839; 29 N-Linked glycans (2 sites).
DR GlyGen; P43307; 7 sites, 34 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P43307; -.
DR MetOSite; P43307; -.
DR PhosphoSitePlus; P43307; -.
DR BioMuta; SSR1; -.
DR DMDM; 22261821; -.
DR CPTAC; CPTAC-593; -.
DR CPTAC; CPTAC-594; -.
DR EPD; P43307; -.
DR jPOST; P43307; -.
DR MassIVE; P43307; -.
DR MaxQB; P43307; -.
DR PaxDb; P43307; -.
DR PeptideAtlas; P43307; -.
DR PRIDE; P43307; -.
DR ProteomicsDB; 55609; -. [P43307-1]
DR ProteomicsDB; 55610; -. [P43307-2]
DR TopDownProteomics; P43307-1; -. [P43307-1]
DR TopDownProteomics; P43307-2; -. [P43307-2]
DR Antibodypedia; 2405; 264 antibodies from 29 providers.
DR DNASU; 6745; -.
DR Ensembl; ENST00000244763.9; ENSP00000244763.4; ENSG00000124783.14. [P43307-1]
DR GeneID; 6745; -.
DR KEGG; hsa:6745; -.
DR MANE-Select; ENST00000244763.9; ENSP00000244763.4; NM_003144.5; NP_003135.2.
DR UCSC; uc003mxf.6; human. [P43307-1]
DR CTD; 6745; -.
DR DisGeNET; 6745; -.
DR GeneCards; SSR1; -.
DR HGNC; HGNC:11323; SSR1.
DR HPA; ENSG00000124783; Low tissue specificity.
DR MIM; 600868; gene.
DR neXtProt; NX_P43307; -.
DR OpenTargets; ENSG00000124783; -.
DR PharmGKB; PA36147; -.
DR VEuPathDB; HostDB:ENSG00000124783; -.
DR eggNOG; KOG1631; Eukaryota.
DR GeneTree; ENSGT00400000022103; -.
DR HOGENOM; CLU_073618_0_0_1; -.
DR InParanoid; P43307; -.
DR OMA; FNFHIQN; -.
DR OrthoDB; 1349929at2759; -.
DR PhylomeDB; P43307; -.
DR TreeFam; TF321074; -.
DR PathwayCommons; P43307; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; P43307; -.
DR BioGRID-ORCS; 6745; 29 hits in 1088 CRISPR screens.
DR ChiTaRS; SSR1; human.
DR GeneWiki; SSR1; -.
DR GenomeRNAi; 6745; -.
DR Pharos; P43307; Tbio.
DR PRO; PR:P43307; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P43307; protein.
DR Bgee; ENSG00000124783; Expressed in corpus epididymis and 213 other tissues.
DR ExpressionAtlas; P43307; baseline and differential.
DR Genevisible; P43307; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR InterPro; IPR005595; TRAP_alpha.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1557127"
FT CHAIN 19..286
FT /note="Translocon-associated protein subunit alpha"
FT /id="PRO_0000033281"
FT TOPO_DOM 19..207
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 39..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 68..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_013621"
FT VARIANT 28
FT /note="L -> S (in dbSNP:rs10004)"
FT /evidence="ECO:0000269|PubMed:8050590, ECO:0000269|Ref.6"
FT /id="VAR_022427"
FT CONFLICT 6
FT /note="R -> G (in Ref. 7; BAC11701)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="E -> A (in Ref. 6; BAD96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Y -> H (in Ref. 1; CAA78290)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="F -> Y (in Ref. 4; BAF84239)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="L -> P (in Ref. 6; BAD96529)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="Q -> R (in Ref. 4; BAF84239)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="E -> D (in Ref. 5; CAG33242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 32235 MW; 2C631DC0CC3EB489 CRC64;
MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE DDEAEVEEDE
PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK
VEMGTSSQND VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE
