ID SEC23_YEAST STANDARD; PRT; 768 AA. AC P15303; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) 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]. 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=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). 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 SEC16. CC -!- INTERACTION: 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 IntAct; P15303; -. DR GermOnline; 144446; -. DR Ensembl; YPR181C; Saccharomyces cerevisiae. DR SGD; S000006385; SEC23. DR LinkHub; P15303; -. DR GO; GO:0030127; C:COPII vesicle coat; TAS. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005096; F:GTPase activator activity; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0006914; P:autophagy; IMP. DR GO; GO:0006888; P:ER to Golgi transport; IMP. DR GO; GO:0030433; P:ER-associated protein catabolism; IMP. 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. KW 3D-structure; Complete proteome; Endoplasmic reticulum; KW ER-Golgi transport; Golgi stack; Protein transport; Transport. FT HELIX 3 10 FT STRAND 12 14 FT STRAND 16 16 FT STRAND 18 20 FT HELIX 23 28 FT TURN 29 29 FT STRAND 34 37 FT TURN 39 40 FT TURN 44 45 FT STRAND 48 49 FT STRAND 55 55 FT TURN 59 61 FT STRAND 64 64 FT TURN 67 68 FT STRAND 71 72 FT TURN 73 76 FT STRAND 77 78 FT TURN 81 83 FT STRAND 88 88 FT HELIX 91 93 FT HELIX 103 105 FT TURN 106 106 FT STRAND 109 113 FT STRAND 123 129 FT HELIX 134 149 FT TURN 150 150 FT TURN 153 154 FT STRAND 156 162 FT STRAND 165 168 FT STRAND 177 183 FT TURN 184 185 FT HELIX 190 198 FT HELIX 224 227 FT STRAND 229 230 FT HELIX 231 243 FT TURN 244 244 FT TURN 254 255 FT STRAND 256 256 FT HELIX 262 276 FT TURN 278 279 FT STRAND 283 288 FT STRAND 303 303 FT TURN 304 305 FT HELIX 311 316 FT TURN 317 317 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 369 372 FT TURN 375 376 FT HELIX 378 386 FT TURN 387 388 FT STRAND 390 390 FT TURN 392 393 FT STRAND 396 396 FT STRAND 399 408 FT TURN 410 411 FT STRAND 412 418 FT STRAND 422 423 FT STRAND 432 432 FT STRAND 439 439 FT STRAND 444 450 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 STRAND 523 523 FT HELIX 525 539 FT TURN 540 541 FT HELIX 545 563 FT STRAND 565 565 FT TURN 568 569 FT HELIX 571 573 FT STRAND 575 575 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 639 640 FT STRAND 644 644 FT HELIX 645 647 FT TURN 650 651 FT STRAND 653 657 FT STRAND 661 666 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 STRAND 729 729 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 //