SC24A_BOVIN
ID SC24A_BOVIN Reviewed; 1099 AA.
AC A6QNT8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein transport protein Sec24A {ECO:0000305};
DE AltName: Full=SEC24-related protein A;
GN Name=SEC24A {ECO:0000250|UniProtKB:O95486};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 for their transport to the Golgi complex.
CC Plays a central role in cargo selection within the COPII complex and
CC together with SEC24B may have a different specificity compared to
CC SEC24C and SEC24D. May package preferentially cargos with cytoplasmic
CC DxE or LxxLE motifs and may also recognize conformational epitopes.
CC {ECO:0000250|UniProtKB:O95486}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1. Interacts with TMED2. Interacts
CC (as part of the Sec23/24 complex) with SEC22B; recruits SEC22B into
CC COPII-coated vesicles for its transport from the endoplasmic reticulum
CC to the Golgi (By similarity). Interacts with STING1; promoting STING1
CC translocation to COPII vesicles in a STEEP1-dependent manner (By
CC similarity). Interacts with TMEM39A (By similarity). Interacts with
CC SACM1L; this interaction is reduced in the absence of TMEM39A (By
CC similarity). Interacts with kinase FAM20C; transport of FAM20C from the
CC endoplasmic reticulum to the Golgi is likely to be mediated by COPII
CC vesicles (By similarity). {ECO:0000250|UniProtKB:O95486}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95486}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95486}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95486}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95486}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O95486}.
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; BC148994; AAI48995.1; -; mRNA.
DR RefSeq; NP_001095319.1; NM_001101849.1.
DR AlphaFoldDB; A6QNT8; -.
DR SMR; A6QNT8; -.
DR STRING; 9913.ENSBTAP00000040703; -.
DR PaxDb; A6QNT8; -.
DR PRIDE; A6QNT8; -.
DR Ensembl; ENSBTAT00000043111; ENSBTAP00000040703; ENSBTAG00000018322.
DR GeneID; 505089; -.
DR KEGG; bta:505089; -.
DR CTD; 10802; -.
DR VEuPathDB; HostDB:ENSBTAG00000018322; -.
DR VGNC; VGNC:34413; SEC24A.
DR eggNOG; KOG1985; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_2_0_1; -.
DR InParanoid; A6QNT8; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR TreeFam; TF350406; -.
DR Reactome; R-BTA-204005; COPII-mediated vesicle transport.
DR Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR Reactome; R-BTA-5694530; Cargo concentration in the ER.
DR Reactome; R-BTA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000018322; Expressed in spiral colon and 110 other tissues.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
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 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.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Metal-binding; Protein transport; Reference proteome; Transport;
KW Zinc.
FT CHAIN 1..1099
FT /note="Protein transport protein Sec24A"
FT /id="PRO_0000311673"
FT REPEAT 972..1044
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..461
FT /note="Zinc finger-like"
FT COMPBIAS 67..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
SQ SEQUENCE 1099 AA; 120097 MW; DD69317C8C747D8E CRC64;
MSQPGIPASG GSSTGLQAQN GAASASGSPY TNGPVQNALM SSQVSVSQGY NSQLPGSYPH
LIPAKTLNPV SGQSNSGGSQ TVSPLSNYQG PGQALYGPPV ASHPVTPSLH SGPSPQMPLP
TSQNPAATPM PSGSFLPGAS VSSPSNWQYN YLSQTNHCPR ASSQPTMTGN TNLMSPQYVS
SGDSSLQNNI IKSGSALPLV NPPLPTTFQP GAPLGPPPTG GPPPVRALTP QKLTPRTMPQ
PSFNSTSNQE GIISNTNNGS MVVHNNYDEI EGGGFLATSQ PTTKNPTMSR SVGYSYPSLP
PGYQNTAPPS TTGAGLPPSS LNYPSGPQAF TQTPLGANHL TSSMSGLSLH PEGLRVINLL
QERNMLPSTP LQPPVPNLHE DIQKLNCNPE LFRCTLTSIP QTQALLNKAK LPLGLLLHPF
KDLVQLPVVT SSTIVRCRSC RTYINPFVSF LDQRRWKCNL CYRVNDVPEE FMYNPLTRVY
GEPHRRPEVQ NATIEFMAPS EYMLRPPQPP VYLFVFDVSH NAIETGYLNS VCQSLLDNLD
LLPGNTRTKI GFITFDSTIH FYSLQEGLSQ PQMLIVSDIE DVFIPMPENL LVNLNESKEL
VQDLLKTLPQ MFTKTLETQS ALGPALQAAF KLMSPTGGRM SVFQTQLPTL GVGALKPREE
PNQRSSAKEI HLTPSTDFYK KLALDCSGQQ VAVDLFLLSG QYSDLASLGC ISRYSAGSVY
YYPSYHHQHN PIQVQKLEKE LQRYLTRKIG FEAVMRIRCT KGLSIHTFHG NFFVRSTDLL
SLPNVNPDAG YAVQMSVEES LTDTQLVSFQ SALLYTSSKG ERRIRVHTLC LPVVSTLNEV
FLGADVQAIS GLLANMAVDR SVTASLSDAR DALVNAVIDS LSAYRSSALS NQQPGLMVPF
SLRLFPLFVL ALLKQKSFQT GTNARLDERI FAMCQVKNQP LVYLMLTTHP SLYRVDNLSD
EGAISINDRT IPQPPILQLS VEKLSRDGAF LMDAGSVLML WVGRNCGQNF LSQVLGVENY
ALIPQTMTDL PELDTPESAR TIAFISWLRE QRPFYPILYV IRDESPMKAN FLQNMVEDRT
ESALSYYEFL LHIQQQVNK
