SC241_SACU7
ID SC241_SACU7 Reviewed; 885 AA.
AC Q876F4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein transport protein SEC24-1;
GN Name=SEC241;
OS Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS uvarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=659244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=623-6C / CBS 9787 / CLIB 533;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
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}.
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; AY144861; AAO32425.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876F4; -.
DR SMR; Q876F4; -.
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 CDD; cd01479; Sec24-like; 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; 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; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
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; Transport;
KW Zinc.
FT CHAIN 1..885
FT /note="Protein transport protein SEC24-1"
FT /id="PRO_0000295498"
FT REGION 164..189
FT /note="Zinc finger-like"
FT REGION 296..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 885 AA; 99690 MW; C3617FB416569E53 CRC64;
MFHHRGGCTP RAQTPYAANV PIVAEQQQFQ QQIDQTANAM GNFQLNDNAY SFTQPAQQPQ
QPSSRKVANQ LYPVDLFTEL PPPIRDLSLP PPPITISQDS IVTPSETSNV PYQYVRSTLN
AVPKTSSLLK KTKLPFGIVI RPYLNLQDSS EYVPLNNDGI IVRCRRCRSY LNPFVAFIEQ
GRRWQCNICR FKNDVPFGFD QNLQGAPINR YERNEIKHSV MEYLAPIEYS VREPPPSTYV
FILDVSQNAV RNGLLATSAR TILENLESLP NHDGRTSVSI ICVDHALHYF YVPLDDDYEE
SDDDDDEDDD DEEEDNEEEE EEEEDEEDDD DSITEAIQMF DVGDLSEPFL PMPSEELVVP
LRYCKKNLEK LLKTIPEVFQ DTHISKFALG PALKAASYLI SNTGGKIEVI SSTLPDTGVG
KLKRRAEQGV LNTTKESSQL LSCQDSFYKT FTIECSKMQI TVDMFLASEE YMDVATLSHL
SRFSGGQTHF YPGFNATSLN DVTKFTRELS KHLSMDISME AVMRVRGSTG LRATSFFGHF
FNRSSDLCAF STMPRDQSYL FEISIEDSLV AEHCYLQVST LLTLNTGERR IRVMTLALPT
TESGREVYAS ADQLAITDFI TQNAVAKALN SSMDSARDLI TKSLQDILSA YKKEISMSNI
TAVTSLNLCA NLRMLPLLMN ALGKHIAFRP GMVPSDYRAS SLNKLETEPL HYLIKSIYPT
VYSLHDIPDE VGLLDSNRET KLPDPINATA SLFERYGLYL IDNSTELFLW VGGDAVPELL
NDVFNTDNIS NVPVGKSELP VLIDSPFNVR LRNIISKIRE NNDTITFQSL YTIRGPSINE
PANLTAEREM ASLRLWVSST LVEDKILNCA SYREYLQSMK TAINR
