SSRA_DICDI
ID SSRA_DICDI Reviewed; 236 AA.
AC Q54R45;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
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; ORFNames=DDB_G0283497;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of TRAP-alpha, TRAP-beta and TRAP-gamma.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
CC being highly negatively charged, and the cytoplasmic C-terminus
CC positively charged. {ECO:0000250}.
CC -!- PTM: Phosphorylated in its cytoplasmic tail. {ECO:0000250}.
CC -!- MISCELLANEOUS: Seems to bind calcium. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAP-alpha family. {ECO:0000305}.
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DR EMBL; AAFI02000055; EAL65733.1; -; Genomic_DNA.
DR RefSeq; XP_639046.1; XM_633954.1.
DR AlphaFoldDB; Q54R45; -.
DR STRING; 44689.DDB0266492; -.
DR PaxDb; Q54R45; -.
DR EnsemblProtists; EAL65733; EAL65733; DDB_G0283497.
DR GeneID; 8624071; -.
DR KEGG; ddi:DDB_G0283497; -.
DR dictyBase; DDB_G0283497; ssr1.
DR eggNOG; KOG1631; Eukaryota.
DR HOGENOM; CLU_073618_2_0_1; -.
DR InParanoid; Q54R45; -.
DR OMA; FNFHIQN; -.
DR PhylomeDB; Q54R45; -.
DR PRO; PR:Q54R45; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR InterPro; IPR005595; TRAP_alpha.
DR Pfam; PF03896; TRAP_alpha; 1.
PE 3: Inferred from homology;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..236
FT /note="Translocon-associated protein subunit alpha"
FT /id="PRO_0000330738"
FT TOPO_DOM 21..163
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 236 AA; 26252 MW; DBDCFBE6624577E2 CRC64;
MNKLITLLLA VLMIISCVYS DDVEITDDEV VQATPTSDVS FSYIFPDNQD KNFAAGSVVE
VLVGFTNNAD KALNITHIFA SLNHPQDFSV FIQNYTRGDF GIAVEKGHHA TLAYRFVPSE
YLEPREFGLL ISLEYQDGAQ NFTQTFFNST INITEKETSF DMDSFFLILL GLGFVGGIGY
IVYGKMPKQK KVRTVSKVNK NAVRVETEDE TAEWLSGTSA ASSKVKSVQK VVKKNK