SEC24_LACK1
ID SEC24_LACK1 Reviewed; 886 AA.
AC Q875Q0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Protein transport protein SEC24;
DE Flags: Fragment;
GN Name=SEC24;
OS Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=226302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC / NRRL Y-12651;
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}.
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DR EMBL; AY145019; AAO32581.1; -; Genomic_DNA.
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..>886
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295502"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..245
FT /note="Zinc finger-like"
FT COMPBIAS 86..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT NON_TER 886
SQ SEQUENCE 886 AA; 98238 MW; C99BDE8FF5B5FCA7 CRC64;
MSGHRKRVYP QSQFQYANSV PAAGQAAAPG YPPVAGMPQA DYSQQAQPQA QPAFLTPAQQ
QLHQQIDQAV QGVGNMQLHN VPVVDPNGFY QQQPPVTTPG AVPSGAVPQM QQQYAQPAAI
GKAMNQLYPI DLLTELPPPI SDLSLPPPPL MVPPEKFVVP SETANAPPDF LRCTLNALPK
SNSLLKKSKL PLALVIRPYQ CLSDSQNPIP LTSDGXXVRC RRCRSYINPF VTFVEGGRRW
RCNFCNLAND VPMAFDMSTQ GVPTNRYERN EVQHSVVEYL APREYAVRAP PPSVYSFILD
VSQNAIKNGL LATAARTLLE TLDTLPNHDD RTRISILAVD NSIHYFSIPT DEEGDHIKML
DVVDLDEPFL PMPDSLFVSL SECRSNLEKL LSQLPEIFQY NIMNKFALGP ALKAAHNLIK
RIGGKIIVVS STLPNIGVGK LSKRNEAGVA NTSKEASQLL SVQDSFYKNF TIDCNKTQVT
IDLFLASDDY MDVASLSNLA RYTSGQTHFY PGWSAAKLTD VTKFTKEFSK HLSMDLSMEA
VMRARGSSGL RMSRFYGHFF NRSSDLCAFP TFPRDQSYVF EVNLDEQIVR DYAYLQVAVL
LSSNTAQRRI RVITICIPTT ESLPEVYASA DQLAITAYFA QKAIEKVFSS GFEDAREFLN
KSVQDILATY KKDIVVSNTA GGAPLRLCAN LRMFPLLMHS LTKHMAFRNG IVPSDHRAAA
LNNLESMPLP YLIKNIYATV YSLHDMPDEA GLQNENGEVV LPEPINATSS LLERYGLYLI
DNASELFLWI GGDAVNELTM DVFGTPEILQ IPIGKNELPV LENSEFNARV RNIISKIREH
SDIITYQSLY IVMGASLSEP VNHASAREVA TLRLWATSTL VEDKVL
