(data stored in ACNUC7421 zone)

SWISSPROT: SEC23_ASHGO

ID   SEC23_ASHGO             Reviewed;         756 AA.
AC   Q758M7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Protein transport protein SEC23;
GN   Name=SEC23; OrderedLocusNames=AEL272W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC       promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles and the
CC       selection of cargo molecules (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC       SEC23/24 complex, the SEC13/31 complex, and the protein SAR1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC       COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic
CC       reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC       {ECO:0000305}.
DR   EMBL; AE016818; AAS52412.1; -; Genomic_DNA.
DR   RefSeq; NP_984588.1; NM_209941.1.
DR   SMR; Q758M7; -.
DR   STRING; 33169.AAS52412; -.
DR   PRIDE; Q758M7; -.
DR   EnsemblFungi; AAS52412; AAS52412; AGOS_AEL272W.
DR   GeneID; 4620768; -.
DR   KEGG; ago:AGOS_AEL272W; -.
DR   HOGENOM; HOG000231690; -.
DR   InParanoid; Q758M7; -.
DR   KO; K14006; -.
DR   OMA; SLKVFME; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0003400; P:regulation of COPII vesicle coating; IEA:EnsemblFungi.
DR   GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR   CDD; cd11287; Sec23_C; 1.
DR   Gene3D; 3.40.20.10; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR037364; Sec23.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR037550; Sec23_C.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR11141; PTHR11141; 1.
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   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF81811; SSF81811; 1.
DR   SUPFAM; SSF82754; SSF82754; 1.
DR   SUPFAM; SSF82919; SSF82919; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758M7.
DR   SWISS-2DPAGE; Q758M7.
KW   Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..756
FT                   /note="Protein transport protein SEC23"
FT                   /id="PRO_0000295449"
FT   METAL           56
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           61
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           80
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           83
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   756 AA;  83993 MW;  468DEE2DD6DD5CB3 CRC64;
     MDFEQNEDIN GVRFSWNVFP ASRTDANKNV VPVGCLYTPL KEIEELAVVS YNPVVCGGPH
     CKAVLNPYCE IDVRSNVWAC PLCGTRNHLP QHYANMSQEA MPAELNSTTV EYITNRPVQV
     APIFFYVVDV TAEEENLQAL KDSIITSLSL LPPNALVGLI TYGNVVQLHD LSCTAIDKCN
     VFRGDREYQL QQLVEMLTGE KSGGNLSAGP QMKITPFSLN RFFLPLEHVE FKLTQLLENL
     RPDQWTIPPG HRPLRATGSA LNIATLLLQG CYRHVAARIC LFASGPGTVA PGMIVSSELK
     DPLRSHHDID SDNAKHHKKA CKFYNQLAER AAENGHTIDI FAGCYDQVGM SEMKKLTDST
     GGVLLLTDAF STAIFKQSFI RLFSKDEEGY LTMAFNASMC IKTSADLKLQ GLIGHASPVN
     VDAQNVSDSE IGIGGTSTWK MASLSPHHSY AIFFEIANTA ATASLMGDRP KLAYTQFITA
     YQHASGTNRV RVTTVANQML PFGNPAIAAS FDQEAAAVLM ARVAVDKADS DDGADVIRWI
     DRTLIKLCQK YADYNKGDPR SFRLAPNFSL YPQFIYYLRR SQFLSVFNNS PDETAFYRHI
     FTREDTTNSL IMIQPTLTSF SMEEEPQPVL LDSVSVKPNT ILLLDTFFYI LIYHGEQIAQ
     WRKAGYQDDP QYADFKSLLE EPKLEAAELL VDRFPLPRFI DTEAGGSQAR FLLSKLNPSD
     SYQNQSAAGS TIVLTDDVSL QNFMIHLQDV CVNGQN
//

If you have problems or comments...

PBIL Back to PBIL home page