SC242_SACU7
ID SC242_SACU7 Reviewed; 926 AA.
AC Q876F5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein transport protein SEC24-2;
GN Name=SEC242;
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; AY144860; AAO32424.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876F5; -.
DR SMR; Q876F5; -.
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..926
FT /note="Protein transport protein SEC24-2"
FT /id="PRO_0000295499"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Zinc finger-like"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 926 AA; 103437 MW; CB6CCDAD424618CF CRC64;
MSHHKKRVYP QAQAQYGQSA TPLQQPAQLV PPQDPAAAGM SYAQMGMPPQ GAAAPMGQPQ
FLTPAQEQLH QQIDQAATSM NDMHLHNVPL VDPNAYMQQQ VPAQAGMPFQ QQQQPLPAQV
YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP ITDLTLPPPP LVIPPEKMLV PSEVSNASPD
YIRSTLNAVP KNSSLLKKSK LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP
FITFIEQGRR WRCNFCRLAN DVPMQMDQTD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ
PPPATYCFLV DVSQASIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV DNAIHYFKIP
LDSDNNEGST DQINMMDIAD LEEPFLPRPN SMVVSLKACR QNIESLLTKI PQIFQSNLIT
SFALGPALKS AYHLIGGVGG KIIVVSGTLP NLGIGKLQRR NESGVVNTSK ETAQLLSCQD
SFYKNFTIDC SKVQITVDLF LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF
STEFAKHISM DLCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV
DESIMTEYCY IQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA IASFYNSKAV
EKALNSSLDE ARVLINKSVQ DILATYKKEI VVSNTAGGAP LRLCANLRMF PLLMHSLTKH
MAFRSGIVPS DHRASALNIL ESLPLKYLIK NIYPDVYSLH DMADEAGLPL QTEDGETTAT
VVLPQPLNAT SSLFERYGLY LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI
PVVENSEFNQ RVRNIINQLR NHDDIITYQS LYIVRGASLS EPVNHASARE VATLRLWASS
TLVEDKILNN ESYREFLQIM KARISK
