SEC72_YEAST
ID SEC72_YEAST Reviewed; 193 AA.
AC P39742; D6VYT8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Translocation protein SEC72;
DE AltName: Full=Sec62/63 complex 23 kDa subunit;
DE Short=p23;
GN Name=SEC72; Synonyms=SEC67, SIM2; OrderedLocusNames=YLR292C;
GN ORFNames=L8003.18;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC STRAIN=YPH501;
RX PubMed=8051213; DOI=10.1083/jcb.126.4.935;
RA Feldheim D., Schekman R.;
RT "Sec72p contributes to the selective recognition of signal peptides by the
RT secretory polypeptide translocation complex.";
RL J. Cell Biol. 126:935-943(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8441423; DOI=10.1128/mcb.13.3.1920-1932.1993;
RA Bushman J.L., Asuru A.I., Matts R.L., Hinnebusch A.G.;
RT "Evidence that GCD6 and GCD7, translational regulators of GCN4, are
RT subunits of the guanine nucleotide exchange factor for eIF-2 in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:1920-1932(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RX PubMed=8455603; DOI=10.1128/mcb.13.4.2152-2161.1993;
RA Belhumeur P., Lee A., Tam R., Dipaolo T., Fortin N., Clark M.W.;
RT "GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces
RT cerevisiae: GTP-binding proteins involved in the maintenance of nuclear
RT organization.";
RL Mol. Cell. Biol. 13:2152-2161(1993).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH KAR2; SEC63 AND SEC66.
RX PubMed=8253836; DOI=10.1083/jcb.123.6.1355;
RA Brodsky J.L., Schekman R.;
RT "A Sec63p-BiP complex from yeast is required for protein translocation in a
RT reconstituted proteoliposome.";
RL J. Cell Biol. 123:1355-1363(1993).
RN [8]
RP IDENTIFICATION IN THE SEC62/63 COMPLEX.
RX PubMed=2000150; DOI=10.1038/349806a0;
RA Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.;
RT "Assembly of yeast Sec proteins involved in translocation into the
RT endoplasmic reticulum into a membrane-bound multisubunit complex.";
RL Nature 349:806-808(1991).
RN [9]
RP ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
RX PubMed=7758110; DOI=10.1016/0092-8674(95)90077-2;
RA Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.;
RT "Posttranslational protein transport in yeast reconstituted with a purified
RT complex of Sec proteins and Kar2p.";
RL Cell 81:561-570(1995).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP INTERACTION WITH YLR301W.
RX PubMed=12518317; DOI=10.1002/yea.954;
RA Willer M., Jermy A.J., Young B.P., Stirling C.J.;
RT "Identification of novel protein-protein interactions at the cytosolic
RT surface of the Sec63 complex in the yeast ER membrane.";
RL Yeast 20:133-148(2003).
CC -!- FUNCTION: Acts as non-essential component of the Sec62/63 complex which
CC is involved in SRP-independent post-translational translocation across
CC the endoplasmic reticulum (ER) and functions together with the Sec61
CC complex and KAR2 in a channel-forming translocon complex. A cycle of
CC assembly and disassembly of Sec62/63 complex from SEC61 may govern the
CC activity of the translocon. SEC72 may be involved in signal peptide
CC recognition for a defined subset of leader peptides, or may increase
CC the efficiency of unusual or 'difficult' secretory precursors to the
CC translocation pore, it may be that this protein binds charged leader
CC peptides to the membrane until they engage the translocation apparatus.
CC -!- SUBUNIT: Component of the heterotetrameric Sec62/63complex composed of
CC SEC62, SEC63, SEC71 and SEC72. The Sec62/63 complex associates with the
CC Sec61 complex to form the Sec complex. May interact with protein
CC YLR301W. Part of a complex consisting of KAR2, SEC63, SEC66 and SEC72.
CC {ECO:0000269|PubMed:2000150, ECO:0000269|PubMed:8253836}.
CC -!- INTERACTION:
CC P39742; P14906: SEC63; NbExp=4; IntAct=EBI-16651, EBI-16636;
CC P39742; P33754: SEC66; NbExp=5; IntAct=EBI-16651, EBI-16647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 5290 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L29340; AAA21840.1; -; Genomic_DNA.
DR EMBL; L07116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U17243; AAB67338.1; -; Genomic_DNA.
DR EMBL; AY558214; AAS56540.1; -; Genomic_DNA.
DR EMBL; L08690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006945; DAA09604.1; -; Genomic_DNA.
DR PIR; S50377; A53835.
DR RefSeq; NP_013395.1; NM_001182180.1.
DR PDB; 6N3Q; EM; 3.68 A; F=1-193.
DR PDB; 6ND1; EM; 4.10 A; F=1-193.
DR PDB; 7AFT; EM; 4.40 A; F=1-193.
DR PDB; 7KAH; EM; 3.10 A; F=1-193.
DR PDB; 7KAI; EM; 3.20 A; F=1-193.
DR PDB; 7KAJ; EM; 3.10 A; F=1-193.
DR PDB; 7KAO; EM; 4.00 A; F=1-193.
DR PDB; 7KAP; EM; 4.10 A; F=1-193.
DR PDB; 7KAQ; EM; 4.00 A; F=1-193.
DR PDB; 7KAR; EM; 4.00 A; F=1-193.
DR PDB; 7KAS; EM; 3.90 A; F=1-193.
DR PDB; 7KAT; EM; 4.40 A; F=1-193.
DR PDB; 7KAU; EM; 4.00 A; F=1-193.
DR PDB; 7KB5; EM; 3.80 A; F=1-193.
DR PDBsum; 6N3Q; -.
DR PDBsum; 6ND1; -.
DR PDBsum; 7AFT; -.
DR PDBsum; 7KAH; -.
DR PDBsum; 7KAI; -.
DR PDBsum; 7KAJ; -.
DR PDBsum; 7KAO; -.
DR PDBsum; 7KAP; -.
DR PDBsum; 7KAQ; -.
DR PDBsum; 7KAR; -.
DR PDBsum; 7KAS; -.
DR PDBsum; 7KAT; -.
DR PDBsum; 7KAU; -.
DR PDBsum; 7KB5; -.
DR AlphaFoldDB; P39742; -.
DR SMR; P39742; -.
DR BioGRID; 31558; 257.
DR ComplexPortal; CPX-3055; Translocon complex.
DR ComplexPortal; CPX-3056; SEC62-SEC63 complex.
DR DIP; DIP-2491N; -.
DR IntAct; P39742; 8.
DR MINT; P39742; -.
DR STRING; 4932.YLR292C; -.
DR TCDB; 3.A.5.8.1; the general secretory pathway (sec) family.
DR iPTMnet; P39742; -.
DR MaxQB; P39742; -.
DR PaxDb; P39742; -.
DR PRIDE; P39742; -.
DR EnsemblFungi; YLR292C_mRNA; YLR292C; YLR292C.
DR GeneID; 850999; -.
DR KEGG; sce:YLR292C; -.
DR SGD; S000004283; SEC72.
DR VEuPathDB; FungiDB:YLR292C; -.
DR eggNOG; ENOG502RZEU; Eukaryota.
DR HOGENOM; CLU_111698_0_0_1; -.
DR InParanoid; P39742; -.
DR OMA; KMYTLAI; -.
DR BioCyc; YEAST:G3O-32387-MON; -.
DR PRO; PR:P39742; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P39742; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0031207; C:Sec62/Sec63 complex; IPI:SGD.
DR GO; GO:0071256; C:translocon complex; IPI:ComplexPortal.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IDA:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8051213"
FT CHAIN 2..193
FT /note="Translocation protein SEC72"
FT /id="PRO_0000097664"
FT CONFLICT 33
FT /note="V -> L (in Ref. 1; AAA21840)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="L -> M (in Ref. 1; AAA21840)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7KAH"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7KAJ"
FT HELIX 22..40
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 98..119
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:7KAH"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:7KAH"
SQ SEQUENCE 193 AA; 21607 MW; D5D200DF2DCA81DB CRC64;
MVTLEYNANS KLITASDAVV ALSTETNIDQ INVLTTSLIG ETNPNFTPQP NEALSKMIKG
LFESGMKNLQ QKKLNEALKN VSLAIEMAQR KRAPWEAFAI QLPELHFMLR SKIDLCLILG
KHLEALQDLD FLLGTGLIQP DVFVRKADCL LKLRQWEEAR ATCERGLALA PEDMKLRALL
IETARNLAEY NGE
