SEC23_PICST
ID SEC23_PICST Reviewed; 749 AA.
AC A3GFA2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; ORFNames=PICST_80516;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
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DR EMBL; AAVQ01000001; EAZ63719.2; -; Genomic_DNA.
DR RefSeq; XP_001387742.2; XM_001387705.1.
DR AlphaFoldDB; A3GFA2; -.
DR SMR; A3GFA2; -.
DR STRING; 4924.XP_001387742.2; -.
DR EnsemblFungi; EAZ63719; EAZ63719; PICST_80516.
DR GeneID; 4850951; -.
DR KEGG; pic:PICST_80516; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; A3GFA2; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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;
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..749
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000295470"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 749 AA; 84016 MW; F423086EE02AD598 CRC64;
MNFEEAEDIN GIRFAWNALP STKVEAGKVV VPTGVIYTPL KQREDLPVAV YDPIFCSNQN
CKSILNPYCT IDPSGFWRCP LCSYRNPLPA HYQGVTPENL PLELQPGSST IEYITARPVQ
NPPIFFLLID LCQDEDNLAA LKETLIVSLS LLPPNALIGL ITYGTMVQVH DLGSEKISKS
YIFRGDKEYT EKQISDMLNR PTSTPQGQLP QFANSLTRFF LPVEDVEFQL TSILENLGKD
PWTVANGDRP LRSTGSALNV AANLLGSTFP GFGARIMLFS AGPGTLSPGL IVGPQLKEPI
RSHSDIDKDN AKHFKKAVKF YDSIAAKMVK NAHTVDIFAG CYDQIGMLEM KNLCNLTGGT
LLLSDAFTTS IFKQSFLRLF NKDHEGYLLM GFNGTFDVKT SKELKISGLI GHASSMNVKT
QNVSENELGI GGTSQYRLCS VSPQHSYAVF FDVVNTQSLP QNAQSYTQFI THYQHASGTY
RIRVTTVSNF LTSDEQTLTN SFDQEAAAVL MSRVTLFKSE QDDGADVLRW IDRMLIRLCQ
KFADYRKDQE ESFRLGPQFQ LYPQFIYYLR RSQFLQVFNN SPDETAFYRH VLLTEDTNNS
LIMIQPTLTS FSLDSEPEAV LLDSVSIKDD KILLLDTFFH ILIFHGKTIA QWRKAGYQNQ
PEYENFKLLL EEPKQEAAEL LVDRYPLPRF IDTEEGGSQA RFLYSKLNPS ITYNSSEFAT
NNGAIVLTDD VSLQVFMGHL QKLVVSGSS
