Full text data of SSR1
SSR1
(TRAPA)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Translocon-associated protein subunit alpha; TRAP-alpha (Signal sequence receptor subunit alpha; SSR-alpha; Flags: Precursor)
Translocon-associated protein subunit alpha; TRAP-alpha (Signal sequence receptor subunit alpha; SSR-alpha; Flags: Precursor)
UniProt
P43307
ID SSRA_HUMAN Reviewed; 286 AA.
AC P43307; A8K685; Q53GX2; Q53H19; Q5TAM3; Q6IB43; Q8NBH9; Q96IA2;
read moreAC Q9TNQ8; Q9UN49;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 3.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Kihara A., 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).
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to
CC bind calcium to the ER membrane and thereby regulate the retention
CC of ER resident proteins. May be involved in the recycling of the
CC translocation apparatus after completion of the translocation
CC process or may function as a membrane-bound chaperone facilitating
CC folding of translocated proteins.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
CC TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the
CC interaction is required for efficient folding of glycosylated
CC proteins.
CC -!- INTERACTION:
CC P27824:CANX; NbExp=5; IntAct=EBI-714168, EBI-355947;
CC P01009:SERPINA1; NbExp=4; IntAct=EBI-714168, EBI-986224;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type 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 Note=No experimental confirmation available;
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI16444.1; Type=Erroneous gene model prediction;
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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; CAI16444.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC007710; AAH07710.1; -; mRNA.
DR PIR; I38246; I38246.
DR RefSeq; NP_003135.2; NM_003144.3.
DR UniGene; Hs.114033; -.
DR ProteinModelPortal; P43307; -.
DR IntAct; P43307; 23.
DR MINT; MINT-1379984; -.
DR PhosphoSite; P43307; -.
DR DMDM; 22261821; -.
DR PaxDb; P43307; -.
DR PeptideAtlas; P43307; -.
DR PRIDE; P43307; -.
DR DNASU; 6745; -.
DR Ensembl; ENST00000244763; ENSP00000244763; ENSG00000124783.
DR GeneID; 6745; -.
DR KEGG; hsa:6745; -.
DR UCSC; uc003mxf.4; human.
DR CTD; 6745; -.
DR GeneCards; GC06M007232; -.
DR HGNC; HGNC:11323; SSR1.
DR HPA; HPA011276; -.
DR HPA; HPA017062; -.
DR MIM; 600868; gene.
DR neXtProt; NX_P43307; -.
DR PharmGKB; PA36147; -.
DR eggNOG; NOG127973; -.
DR HOVERGEN; HBG009736; -.
DR KO; K13249; -.
DR PhylomeDB; P43307; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SSR1; human.
DR GeneWiki; SSR1; -.
DR GenomeRNAi; 6745; -.
DR NextBio; 26310; -.
DR PRO; PR:P43307; -.
DR ArrayExpress; P43307; -.
DR Bgee; P43307; -.
DR Genevestigator; P43307; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR005595; TRAP_alpha.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 18
FT CHAIN 19 286 Translocon-associated protein subunit
FT alpha.
FT /FTId=PRO_0000033281.
FT TOPO_DOM 19 207 Lumenal (Potential).
FT TRANSMEM 208 228 Helical; (Potential).
FT TOPO_DOM 229 286 Cytoplasmic (Potential).
FT MOD_RES 247 247 Phosphoserine.
FT MOD_RES 260 260 Phosphothreonine.
FT MOD_RES 268 268 Phosphoserine.
FT CARBOHYD 136 136 N-linked (GlcNAc...).
FT CARBOHYD 191 191 N-linked (GlcNAc...).
FT VAR_SEQ 68 94 Missing (in isoform 2).
FT /FTId=VSP_013621.
FT VARIANT 28 28 L -> S (in dbSNP:rs10004).
FT /FTId=VAR_022427.
FT CONFLICT 6 6 R -> G (in Ref. 7; BAC11701).
FT CONFLICT 37 37 E -> A (in Ref. 6; BAD96529).
FT CONFLICT 130 130 Y -> H (in Ref. 1; CAA78290).
FT CONFLICT 190 190 F -> Y (in Ref. 4; BAF84239).
FT CONFLICT 220 220 L -> P (in Ref. 6; BAD96529).
FT CONFLICT 263 263 Q -> R (in Ref. 4; BAF84239).
FT CONFLICT 286 286 E -> D (in Ref. 5; CAG33242).
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
//
ID SSRA_HUMAN Reviewed; 286 AA.
AC P43307; A8K685; Q53GX2; Q53H19; Q5TAM3; Q6IB43; Q8NBH9; Q96IA2;
read moreAC Q9TNQ8; Q9UN49;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 3.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Kihara A., 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).
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to
CC bind calcium to the ER membrane and thereby regulate the retention
CC of ER resident proteins. May be involved in the recycling of the
CC translocation apparatus after completion of the translocation
CC process or may function as a membrane-bound chaperone facilitating
CC folding of translocated proteins.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
CC TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the
CC interaction is required for efficient folding of glycosylated
CC proteins.
CC -!- INTERACTION:
CC P27824:CANX; NbExp=5; IntAct=EBI-714168, EBI-355947;
CC P01009:SERPINA1; NbExp=4; IntAct=EBI-714168, EBI-986224;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type 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 Note=No experimental confirmation available;
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI16444.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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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; CAI16444.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC007710; AAH07710.1; -; mRNA.
DR PIR; I38246; I38246.
DR RefSeq; NP_003135.2; NM_003144.3.
DR UniGene; Hs.114033; -.
DR ProteinModelPortal; P43307; -.
DR IntAct; P43307; 23.
DR MINT; MINT-1379984; -.
DR PhosphoSite; P43307; -.
DR DMDM; 22261821; -.
DR PaxDb; P43307; -.
DR PeptideAtlas; P43307; -.
DR PRIDE; P43307; -.
DR DNASU; 6745; -.
DR Ensembl; ENST00000244763; ENSP00000244763; ENSG00000124783.
DR GeneID; 6745; -.
DR KEGG; hsa:6745; -.
DR UCSC; uc003mxf.4; human.
DR CTD; 6745; -.
DR GeneCards; GC06M007232; -.
DR HGNC; HGNC:11323; SSR1.
DR HPA; HPA011276; -.
DR HPA; HPA017062; -.
DR MIM; 600868; gene.
DR neXtProt; NX_P43307; -.
DR PharmGKB; PA36147; -.
DR eggNOG; NOG127973; -.
DR HOVERGEN; HBG009736; -.
DR KO; K13249; -.
DR PhylomeDB; P43307; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SSR1; human.
DR GeneWiki; SSR1; -.
DR GenomeRNAi; 6745; -.
DR NextBio; 26310; -.
DR PRO; PR:P43307; -.
DR ArrayExpress; P43307; -.
DR Bgee; P43307; -.
DR Genevestigator; P43307; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR005595; TRAP_alpha.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 18
FT CHAIN 19 286 Translocon-associated protein subunit
FT alpha.
FT /FTId=PRO_0000033281.
FT TOPO_DOM 19 207 Lumenal (Potential).
FT TRANSMEM 208 228 Helical; (Potential).
FT TOPO_DOM 229 286 Cytoplasmic (Potential).
FT MOD_RES 247 247 Phosphoserine.
FT MOD_RES 260 260 Phosphothreonine.
FT MOD_RES 268 268 Phosphoserine.
FT CARBOHYD 136 136 N-linked (GlcNAc...).
FT CARBOHYD 191 191 N-linked (GlcNAc...).
FT VAR_SEQ 68 94 Missing (in isoform 2).
FT /FTId=VSP_013621.
FT VARIANT 28 28 L -> S (in dbSNP:rs10004).
FT /FTId=VAR_022427.
FT CONFLICT 6 6 R -> G (in Ref. 7; BAC11701).
FT CONFLICT 37 37 E -> A (in Ref. 6; BAD96529).
FT CONFLICT 130 130 Y -> H (in Ref. 1; CAA78290).
FT CONFLICT 190 190 F -> Y (in Ref. 4; BAF84239).
FT CONFLICT 220 220 L -> P (in Ref. 6; BAD96529).
FT CONFLICT 263 263 Q -> R (in Ref. 4; BAF84239).
FT CONFLICT 286 286 E -> D (in Ref. 5; CAG33242).
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
//
MIM
600868
*RECORD*
*FIELD* NO
600868
*FIELD* TI
*600868 SIGNAL SEQUENCE RECEPTOR, ALPHA; SSR1
*FIELD* TX
DESCRIPTION
Transport of secretory and membrane proteins across the endoplasmic
read morereticulum (ER) is thought to be mediated by a complex protein structure
in the membrane called the translocon. SSR1 encodes the alpha subunit of
the translocon-associated membrane protein (TRAP) complex and is found
in close proximity of nascent polypeptide chains translocating across
the ER membrane (summary by Hartmann and Prehn, 1994).
CLONING
By screening a HeLa cell cDNA library using canine TRAP-alpha as probe,
Hartmann and Prehn (1994) cloned human SSR1, which they called
TRAP-alpha. The deduced 286-amino acid human protein contains an
N-terminal signal sequence, followed by an acidic region, 2
glycosylation sites, a transmembrane domain, and 2 basic regions near
the C terminus. Human and canine TRAP-alpha share 96% amino acid
sequence identity. Hartmann and Prehn (1994) also identified TRAP-alpha
sequences in trout, A. thaliana, and rice.
Using RACE, Hirama et al. (1999) cloned full-length human TRAP-alpha, as
well as several variants resulting from alternative polyadenylation.
None of the predicted polyadenylation signals in the TRAP-alpha
transcripts were canonical. The deduced full-length TRAP-alpha protein
contains 286 amino acids. Northern blot analysis of the human myeloid
and osteosarcoma cell lines detected a 3.3-kb TRAP-alpha transcript and
several smaller transcripts.
GENE FUNCTION
Using differential display, Hirama et al. (1999) found that TRAP-alpha
was induced in a growth factor-dependent human myeloid cell line after
stimulation with GMCSF (CSF2; 138960). Cell cycle analysis of human
osteosarcoma cells showed that TRAP-alpha was downregulated in quiescent
cells.
MAPPING
Using radiation hybrid analysis, Hirama et al. (1999) mapped the SSR1
gene to chromosome 6p. Gross (2012) mapped the SSR1 gene to chromosome
6p24.3 based on an alignment of the SSR1 sequence (GenBank GENBANK
AF156965) with the genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/22/2012.
2. Hartmann, E.; Prehn, S.: The N-terminal region of the alpha-subunit
of the TRAP complex has a conserved cluster of negative charges. FEBS
Lett. 349: 324-326, 1994.
3. Hirama, T.; Miller, C. W.; Koeffler, H. P.: Translocon-associated
protein alpha transcripts are induced by granulocyte-macrophage colony-stimulating
factor and exhibit complex alternative polyadenylation. FEBS Lett. 455:
223-227, 1999.
*FIELD* CN
Matthew B. Gross - updated: 06/22/2012
*FIELD* CD
Victor A. McKusick: 10/16/1995
*FIELD* ED
mgross: 06/22/2012
mark: 10/16/1995
*RECORD*
*FIELD* NO
600868
*FIELD* TI
*600868 SIGNAL SEQUENCE RECEPTOR, ALPHA; SSR1
*FIELD* TX
DESCRIPTION
Transport of secretory and membrane proteins across the endoplasmic
read morereticulum (ER) is thought to be mediated by a complex protein structure
in the membrane called the translocon. SSR1 encodes the alpha subunit of
the translocon-associated membrane protein (TRAP) complex and is found
in close proximity of nascent polypeptide chains translocating across
the ER membrane (summary by Hartmann and Prehn, 1994).
CLONING
By screening a HeLa cell cDNA library using canine TRAP-alpha as probe,
Hartmann and Prehn (1994) cloned human SSR1, which they called
TRAP-alpha. The deduced 286-amino acid human protein contains an
N-terminal signal sequence, followed by an acidic region, 2
glycosylation sites, a transmembrane domain, and 2 basic regions near
the C terminus. Human and canine TRAP-alpha share 96% amino acid
sequence identity. Hartmann and Prehn (1994) also identified TRAP-alpha
sequences in trout, A. thaliana, and rice.
Using RACE, Hirama et al. (1999) cloned full-length human TRAP-alpha, as
well as several variants resulting from alternative polyadenylation.
None of the predicted polyadenylation signals in the TRAP-alpha
transcripts were canonical. The deduced full-length TRAP-alpha protein
contains 286 amino acids. Northern blot analysis of the human myeloid
and osteosarcoma cell lines detected a 3.3-kb TRAP-alpha transcript and
several smaller transcripts.
GENE FUNCTION
Using differential display, Hirama et al. (1999) found that TRAP-alpha
was induced in a growth factor-dependent human myeloid cell line after
stimulation with GMCSF (CSF2; 138960). Cell cycle analysis of human
osteosarcoma cells showed that TRAP-alpha was downregulated in quiescent
cells.
MAPPING
Using radiation hybrid analysis, Hirama et al. (1999) mapped the SSR1
gene to chromosome 6p. Gross (2012) mapped the SSR1 gene to chromosome
6p24.3 based on an alignment of the SSR1 sequence (GenBank GENBANK
AF156965) with the genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/22/2012.
2. Hartmann, E.; Prehn, S.: The N-terminal region of the alpha-subunit
of the TRAP complex has a conserved cluster of negative charges. FEBS
Lett. 349: 324-326, 1994.
3. Hirama, T.; Miller, C. W.; Koeffler, H. P.: Translocon-associated
protein alpha transcripts are induced by granulocyte-macrophage colony-stimulating
factor and exhibit complex alternative polyadenylation. FEBS Lett. 455:
223-227, 1999.
*FIELD* CN
Matthew B. Gross - updated: 06/22/2012
*FIELD* CD
Victor A. McKusick: 10/16/1995
*FIELD* ED
mgross: 06/22/2012
mark: 10/16/1995