SEC24_PICST
ID SEC24_PICST Reviewed; 907 AA.
AC A3LRW3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; ORFNames=PICST_88354;
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. Golgi
CC apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
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. SEC24 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000497; ABN65461.2; -; Genomic_DNA.
DR RefSeq; XP_001383490.2; XM_001383453.1.
DR AlphaFoldDB; A3LRW3; -.
DR SMR; A3LRW3; -.
DR STRING; 4924.XP_001383490.2; -.
DR EnsemblFungi; ABN65461; ABN65461; PICST_88354.
DR GeneID; 4837868; -.
DR KEGG; pic:PICST_88354; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; A3LRW3; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000002258; Chromosome 3.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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; IPR036180; Gelsolin-like_dom_sf.
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; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
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..907
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295496"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..232
FT /note="Zinc finger-like"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 907 AA; 99941 MW; 0686DDB48C6ABD31 CRC64;
MSSKRRAYPQ PSYTNGPGSQ LGTPPVAGGF QQPNYGVDQL NQQFQGMNVD PNQAAVAGAP
QAAAGSPYGY NQYQQPGANA NAAHQSRAGN AAGASSYYLQ QGNINAALPL NQLYTTDLSR
ELPPPISDLS LPPPPIVLPA GTTLIPNSET ANAQPEYFRS TLNVIPTNSS LLKKSKLPLA
LVVKPYNALK VEQEDVPVTS DTTISRCRRC RGYINPFVTL AENGRRWRCN FCNLLNDIPS
SFEYDEISGT VKNKFDRVEL NNAVVEFIAP KEYMARAPQP IVYTFIIDVS INAVQSGLTG
TITRTILESL DRIPNKTKTA RVAFIGVDSN LHYFRFNEGL DGTEVLIVSD IDEPFLPSPD
GLLVNLDENR QAVEKLLIDF PSYFEDTANQ GFALGPALKS GHKMISHIGG KLVCFSATLP
NIGEGKLSVR DEASVSGKPK EAKTLLSSAD SFYKSFAVNC NSSQISVDLF LTSSSYQDVA
TLSNLPRFTA GQSHFYPAWT SAKNEDVTKL SKEVSDHLSQ DIALEAVLRV RGSTGIRMSS
FYGNFFNRSS DLCSFPTFPR DQSYVIEMSI EENINKPVVY FQAAVLHSTS FGERRIRVMN
LAIPTSSKLN DIYASADQLA ITNIFTHKAI ETALSSSLPD ARDFLVNKVV DILNVYKKEL
VAGNVSGASP LQLSTNLRML PILLFSLTKH LGFRADRVPS DHRAAALNNL GSLPIPYLVK
YIYPTVYALH TMPDECGLPE KLIQVNEETG EEEEVISTNI MLPEPINDSK SSWENYGLYL
IDNSSELFLW VSGNVVPGLV QDLFGTDNLY AIPTGKTELP EFSDEESEFN FRVRQIIGKI
RENNDSIVWK NLYVVVGGSS NEPIEISQQR DLMALRMWAY SCLVEDKTGS EPSYRDFLTN
LKTKVSQ
