SC61A_DICDI
ID SC61A_DICDI Reviewed; 475 AA.
AC Q54XK2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein transport protein Sec61 subunit alpha;
DE AltName: Full=Secretory 61 complex subunit alpha;
GN Name=sec61a; ORFNames=DDB_G0278885;
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: Appears to play a crucial role in the insertion of secretory
CC and membrane polypeptides into the ER. It is required for assembly of
CC membrane and secretory proteins. Found to be tightly associated with
CC membrane-bound ribosomes, either directly or through adaptor proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and
CC SEC61-gamma. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AAFI02000024; EAL68044.1; -; Genomic_DNA.
DR RefSeq; XP_647801.1; XM_642709.1.
DR AlphaFoldDB; Q54XK2; -.
DR SMR; Q54XK2; -.
DR STRING; 44689.DDB0235193; -.
DR PaxDb; Q54XK2; -.
DR EnsemblProtists; EAL68044; EAL68044; DDB_G0278885.
DR GeneID; 8621759; -.
DR KEGG; ddi:DDB_G0278885; -.
DR dictyBase; DDB_G0278885; sec61a.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_0_1; -.
DR InParanoid; Q54XK2; -.
DR OMA; KWGIGSG; -.
DR PhylomeDB; Q54XK2; -.
DR PRO; PR:Q54XK2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015450; F:protein-transporting ATPase activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..475
FT /note="Protein transport protein Sec61 subunit alpha"
FT /id="PRO_0000328185"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..75
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..145
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..241
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..353
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..440
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 475 AA; 52490 MW; 726D28922092B70A CRC64;
MGFRFLDIVK PFTSLVPEVG QPDRKIPFRE KVLWTAICLF IFLVCSQIPL YGIRSTDSSD
PFYWAKVIMA SNRGTLMELG ISPIVTSGMV MQLLAGAKLI EIDQSVKADR DLFSAAQKLF
GMLICVGQGV AYIWSGSYGD PAVLGFGNCF LIVLQLFFAG IIVMLLDELL QKGYGIGSGI
SLFIATNICE TIVWKTFSPT TVSVGKGTEF EGAVIALFHL LLTRNDKVRA LKEAFYRQNL
PNITNLLATV LIFMVVIYFQ GFRVDLPVKS TRVSGQQGTY PIKLFYTSNI PIILQSALVS
NLYFISQLLY RRFPDNILVN LFGAWRTSEY SQQMIPVSGL TYYISSPNNM SAVLADPFHA
LFYITFMLTS CALFSKVWIE VSGSSARDVA KQLKDQQMTM KGHRDTSVIK ELNRYIPTAA
AFGGLCIGAL TVVADFMGAI GSGTGILLAV TIIYQYFETF VKEQQELSGG IGGLF
