ID A0A093HQ57_STRCA Unreviewed; 1083 AA.
AC A0A093HQ57;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Protein transport protein Sec24A {ECO:0000313|EMBL:KFV84783.1};
DE Flags: Fragment;
GN ORFNames=N308_10621 {ECO:0000313|EMBL:KFV84783.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV84783.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV84783.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV84783.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated
CC vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000256|ARBA:ARBA00008334}.
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DR EMBL; KL206667; KFV84783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HQ57; -.
DR STRING; 441894.ENSSCUP00000022006; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum 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; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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 PANTHER; PTHR13803:SF1; PROTEIN TRANSPORT PROTEIN SEC24A; 1.
DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
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; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 418..454
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 491..729
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 734..818
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 829..929
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 955..1021
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV84783.1"
FT NON_TER 1083
FT /evidence="ECO:0000313|EMBL:KFV84783.1"
SQ SEQUENCE 1083 AA; 118607 MW; FBF9D8FCC314AF0A CRC64;
YLSGPVQNQL MHSSDGQGHN PSIPGSYSHQ MPAKVPPHQS SGQYNYSGSQ IASQLNNYQG
PGQILNRPPV APLSGSPVQQ TGSVPQVLSP ALQNSAAVSS AGSFPPAASP AVLSNWQYSQ
TPVSHPVGSQ TSHLAHVTGT VSTQPPSPLS GNTSPPGSYQ YAASPGGPPL QNSYMKPGSA
PPPVTQPLPP LHPPSRPPLG PPPVGGPPLI RPSALTAGPP NSSVSHFTGT VVFIGDAMST
VRDGSVVQNS YDAIEGGGLM ATTHPSPAPP NLKMGKSVGY SYPNLPPGYQ NTSPPGAPGM
QAPALQYPDG AKPFHQPPLG PNHLTASMGG LTLQQEGLRP VNLLQERNIL PTTLLQAPVP
NLHEDIQKLN CNPELFRCTL TNIPQTQALL NKAKLPLGLL LHPFKDLSQL PVVTSSTIVR
CRSCRTYINP FVSFLDQRRW KCNLCYRVND VPEEFMYNPV TRAYGEPHKR PEVQNATIEF
MAPSEYMLRP PQPPVYLFVF DVSHNAIETG YLNTVCKTLL DNLDLLPGNT RTKIGFITFD
STIHFYSLQE GLSQPQMLIV SDIEDVFIPM PENLLVNLNE NRELIQDLLK TLPQMFTKSL
ETQSALGPAL QAAFKLMSPT GGRISVFQTQ LPSVGMGALK SREEPNQRAT AKDIHLTPST
DFYKKLALDC SGQQVAVDLF LLSGQYSDLA SLGCISRYSA GSVYYYQSYH HKHNPVQVEK
LEKELKRYLT RKIGFEAVMR IRCTKGLSIH TFHGNFFVRS TDLLSLPNVN PDAGYAVQMS
VEESLTDMQV VSFQSALLYT SSKGERRIRV HTMCLPVVTT LSDVYLGADV QAITGLLANM
AVDRSVSASL SDARDALVNA VIDSLSAYRS SVLSIQQPGL MAPRSLRLFP LYVLALLKQK
AFQTGTNARL DERIFTMCQV KNQPLVYLML MTHPNLYRVD DLTDEGALNI NDRTIPQPPI
LQLSVEKLSR DGAYLMDAGS VMFLWIGKNC GQNFISQVLG VPSYASIPQN MTHLPELETA
ESIRTIAFIS WLREQRPFFP ILYIIKDESP LKSSFLQNMI EDRTESALSY YEFLLHIQQQ
VNK
//
