Q9CY50 (SSRA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Translocon-associated protein subunit alpha
Short name=TRAP-alpha

Alternative name(s):
Signal sequence receptor subunit alpha
Short name=SSR-alpha

Gene names

Name:

Ssr1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.
Subunit structure	Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the interaction is required for efficient folding of glycosylated proteins By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity.
Domain	Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.
Miscellaneous	Seems to bind calcium By similarity.
Sequence similarities	Belongs to the TRAP-alpha family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	Calcium
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 286	265	Translocon-associated protein subunit alpha		PRO_0000033282
Regions
	Topological domain	22 – 207	186	Lumenal Potential
	Transmembrane	208 – 228	21	Helical; Potential
	Topological domain	229 – 286	58	Cytoplasmic Potential
Amino acid modifications
	Modified residue	247	1	Phosphoserine By similarity
	Modified residue	260	1	Phosphothreonine Ref.4
	Modified residue	268	1	Phosphoserine Ref.6
	Glycosylation	136	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	143	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	191	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	27	1	G → V in AAK16151. Ref.1
	Sequence conflict	27	1	G → V in AAK82421. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9CY50 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 780D1C6880700C8D	FASTA	286	32,065
	10 20 30 40 50 60 MRLLPRLLLL FLLAFPAAVL LRGGPGGSLA LAQDPTEDEE IVEDSIIEDE DDEAEVEEDE 70 80 90 100 110 120 PTDLAEDKEE EDVSSEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL 130 140 150 160 170 180 DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL 190 200 210 220 230 240 NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VVVGLHQLLE SRKRKRPIQK 250 260 270 280 VEMGTSSQND VDMSWIPQET LNQINKASPR RQPRKRAQKR SVGSDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mus musculus TRAP alpha cDNA." Mesbah K., Babinet C., Barra J. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Embryonic liver and Mammary gland.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary tumor.
[4]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260, MASS SPECTROMETRY. Tissue: Liver.
[5]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-143, MASS SPECTROMETRY. Tissue: Myoblast.
[6]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF326229 mRNA. Translation: AAK16151.2. AF395811 mRNA. Translation: AAK82421.1. AK010884 mRNA. Translation: BAB27245.1. AK166235 mRNA. Translation: BAE38650.1. AK167793 mRNA. Translation: BAE39823.1. BC011255 mRNA. Translation: AAH11255.1.
IPI	IPI00755329.
RefSeq	NP_080241.3. NM_025965.3.
UniGene	Mm.426670. Mm.490298.
3D structure databases
ProteinModelPortal	Q9CY50.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CY50. 2 interactions.
MINT	MINT-1853906.
PTM databases
PhosphoSite	Q9CY50.
Proteomic databases
PaxDb	Q9CY50.
PRIDE	Q9CY50.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021864; ENSMUSP00000021864; ENSMUSG00000021427.
GeneID	107513.
KEGG	mmu:107513.
UCSC	uc011yyk.1. mouse.
Organism-specific databases
CTD	6745.
MGI	MGI:105082. Ssr1.
Phylogenomic databases
eggNOG	NOG127973.
GeneTree	ENSGT00400000022103.
HOGENOM	HOG000006932.
HOVERGEN	HBG009736.
KO	K13249.
OMA	ETIFMYV.
OrthoDB	EOG4M0F2V.
Gene expression databases
Bgee	Q9CY50.
CleanEx	MM_SSR1.
Genevestigator	Q9CY50.
GermOnline	ENSMUSG00000021427. Mus musculus.
Family and domain databases
InterPro	IPR005595. TRAP_alpha. [Graphical view]
Pfam	PF03896. TRAP_alpha. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	358946.
SOURCE	Search...

Entry information

Entry name

SSRA_MOUSE

Accession

Primary (citable) accession number: Q9CY50
Secondary accession number(s): Q3TIM3, Q99MP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program