ID SEC23_YEAST Reviewed; 768 AA. AC P15303; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 06-FEB-2007, entry version 70. DE Protein transport protein SEC23. GN Name=SEC23; OrderedLocusNames=YPR181C; ORFNames=P9705.14; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=MBY8-20C; RX MEDLINE=89356640; PubMed=2670558; RA Hicke L., Schekman R.; RT "Yeast Sec23p acts in the cytoplasm to promote protein transport from RT the endoplasmic reticulum to the Golgi complex in vivo and in vitro."; RL EMBO J. 8:1677-1684(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313271; PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP INTERACTION WITH EMP24. RX PubMed=11560939; DOI=10.1074/jbc.M108113200; RA Belden W.J., Barlowe C.; RT "Distinct roles for the cytoplasmic tail sequences of Emp24p and RT Erv25p in transport between the endoplasmic reticulum and Golgi RT complex."; RL J. Biol. Chem. 276:43040-43048(2001). RN [4] RP FUNCTION, AND INTERACTION WITH GRH1. RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031; RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A., RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., RA Weissman J.S., Krogan N.J.; RT "Exploration of the function and organization of the yeast early RT secretory pathway through an epistatic miniarray profile."; RL Cell 123:507-519(2005). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SAR1 AND ZINC. RX PubMed=12239560; DOI=10.1038/nature01040; RA Bi X., Corpina R.A., Goldberg J.; RT "Structure of the Sec23/24-Sar1 pre-budding complex of the COPII RT vesicle coat."; RL Nature 419:271-277(2002). CC -!- FUNCTION: Component of the COPII coat, that covers ER-derived CC vesicles involved in transport from the endoplasmic reticulum to CC the Golgi apparatus. COPII acts in the cytoplasm to promote the CC transport of secretory, plasma membrane, and vacuolar proteins CC from the endoplasmic reticulum to the Golgi complex. CC -!- SUBUNIT: COPII is composed of at least five proteins: the SEC23/24 CC complex, the SEC13/31 complex and SAR1. Interacts with EMP24, GRH1 CC and SEC16. CC -!- INTERACTION: CC P40482:SEC24; NbExp=1; IntAct=EBI-16584, EBI-16592; CC P53953:SFB2; NbExp=1; IntAct=EBI-16584, EBI-17006; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X15474; CAA33501.1; -; Genomic_DNA. DR EMBL; U25842; AAB68114.1; -; Genomic_DNA. DR PIR; S05742; BVBY23. DR PDB; 1M2O; X-ray; A/C=1-768. DR PDB; 1M2V; X-ray; A=1-768. DR DIP; DIP:2232N; -. DR IntAct; P15303; -. DR Ensembl; YPR181C; Saccharomyces cerevisiae. DR GenomeReviews; U00094_GR; YPR181C. DR KEGG; sce:YPR181C; -. DR SGD; S000006385; SEC23. DR BioCyc; SCER-S28-01:SCER-S28-01-006334-MONOMER; -. DR LinkHub; P15303; -. DR GermOnline; YPR181C; Saccharomyces cerevisiae. DR GO; GO:0030127; C:COPII vesicle coat; TAS:SGD. DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006914; P:autophagy; IMP:SGD. DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD. DR GO; GO:0030433; P:ER-associated protein catabolic process; IMP:SGD. DR InterPro; IPR007123; Gelsoln. DR InterPro; IPR012990; Sec23_24_beta_S. DR InterPro; IPR006900; Sec23_helical. DR InterPro; IPR006896; Sec23_trunk. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR006895; Znf_Sec23_Sec24. DR Pfam; PF00626; Gelsolin; 1. DR Pfam; PF08033; Sec23_BS; 1. DR Pfam; PF04815; Sec23_helical; 1. DR Pfam; PF04811; Sec23_trunk; 1. DR Pfam; PF04810; zf-Sec23_Sec24; 1. DR SMART; SM00327; VWA; 1. KW 3D-structure; Complete proteome; Endoplasmic reticulum; KW ER-Golgi transport; Golgi apparatus; Metal-binding; Protein transport; KW Transport; Zinc. FT CHAIN 1 768 Protein transport protein SEC23. FT /FTId=PRO_0000205145. FT METAL 56 56 Zinc. FT METAL 61 61 Zinc. FT METAL 80 80 Zinc. FT METAL 83 83 Zinc. FT HELIX 3 10 FT STRAND 11 22 FT HELIX 23 28 FT TURN 29 29 FT STRAND 33 37 FT TURN 39 40 FT TURN 44 45 FT TURN 59 61 FT TURN 67 68 FT TURN 73 76 FT TURN 81 83 FT HELIX 91 93 FT HELIX 103 105 FT TURN 106 106 FT STRAND 108 113 FT STRAND 123 129 FT HELIX 134 149 FT TURN 150 150 FT TURN 153 154 FT STRAND 156 168 FT STRAND 172 176 FT STRAND 180 183 FT TURN 184 185 FT HELIX 190 198 FT STRAND 221 223 FT HELIX 224 227 FT STRAND 228 230 FT HELIX 231 243 FT TURN 244 244 FT TURN 254 255 FT HELIX 262 276 FT TURN 278 279 FT STRAND 283 290 FT STRAND 294 297 FT TURN 304 305 FT HELIX 311 315 FT TURN 316 317 FT TURN 320 321 FT HELIX 322 339 FT TURN 340 340 FT STRAND 342 348 FT HELIX 355 365 FT TURN 366 366 FT STRAND 369 373 FT TURN 375 376 FT HELIX 378 386 FT TURN 387 388 FT TURN 392 393 FT STRAND 394 397 FT STRAND 399 408 FT TURN 410 411 FT STRAND 412 420 FT STRAND 437 439 FT STRAND 443 450 FT TURN 452 453 FT STRAND 456 462 FT STRAND 484 495 FT TURN 496 498 FT STRAND 499 512 FT TURN 514 515 FT HELIX 517 521 FT TURN 522 522 FT HELIX 525 539 FT TURN 540 541 FT HELIX 545 563 FT TURN 568 569 FT HELIX 571 573 FT TURN 578 581 FT HELIX 582 592 FT TURN 594 596 FT TURN 599 600 FT HELIX 603 613 FT TURN 614 615 FT HELIX 618 625 FT STRAND 628 632 FT STRAND 634 636 FT HELIX 645 647 FT TURN 650 651 FT STRAND 653 657 FT STRAND 659 666 FT HELIX 668 676 FT TURN 677 677 FT HELIX 678 680 FT TURN 682 683 FT HELIX 685 703 FT TURN 704 704 FT STRAND 710 715 FT TURN 716 717 FT HELIX 719 721 FT HELIX 722 725 FT TURN 726 727 FT HELIX 752 763 SQ SEQUENCE 768 AA; 85385 MW; 69811913848265FB CRC64; MDFETNEDIN GVRFTWNVFP STRSDANSNV VPVGCLYTPL KEYDELNVAP YNPVVCSGPH CKSILNPYCV IDPRNSSWSC PICNSRNHLP PQYTNLSQEN MPLELQSTTI EYITNKPVTV PPIFFFVVDL TSETENLDSL KESIITSLSL LPPNALIGLI TYGNVVQLHD LSSETIDRCN VFRGDREYQL EALTEMLTGQ KPTGPGGAAS HLPNAMNKVT PFSLNRFFLP LEQVEFKLNQ LLENLSPDQW SVPAGHRPLR ATGSALNIAS LLLQGCYKNI PARIILFASG PGTVAPGLIV NSELKDPLRS HHDIDSDHAQ HYKKACKFYN QIAQRVAANG HTVDIFAGCY DQIGMSEMKQ LTDSTGGVLL LTDAFSTAIF KQSYLRLFAK DEEGYLKMAF NGNMAVKTSK DLKVQGLIGH ASAVKKTDAN NISESEIGIG ATSTWKMASL SPYHSYAIFF EIANTAANSN PMMSAPGSAD RPHLAYTQFI TTYQHSSGTN RIRVTTVANQ LLPFGTPAIA ASFDQEAAAV LMARIAVHKA ETDDGADVIR WLDRTLIKLC QKYADYNKDD PQSFRLAPNF SLYPQFTYYL RRSQFLSVFN NSPDETAFYR HIFTREDTTN SLIMIQPTLT SFSMEDDPQP VLLDSISVKP NTILLLDTFF FILIYHGEQI AQWRKAGYQD DPQYADFKAL LEEPKLEAAE LLVDRFPLPR FIDTEAGGSQ ARFLLSKLNP SDNYQDMARG GSTIVLTDDV SLQNFMTHLQ QVAVSGQA //