SEC24_ASPTN
ID SEC24_ASPTN Reviewed; 904 AA.
AC Q0CSL7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein transport protein sec24;
GN Name=sec24; ORFNames=ATEG_03317;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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 (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; CH476597; EAU36591.1; -; Genomic_DNA.
DR RefSeq; XP_001212495.1; XM_001212495.1.
DR AlphaFoldDB; Q0CSL7; -.
DR SMR; Q0CSL7; -.
DR STRING; 341663.Q0CSL7; -.
DR EnsemblFungi; EAU36591; EAU36591; ATEG_03317.
DR GeneID; 4318094; -.
DR VEuPathDB; FungiDB:ATEG_03317; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:EnsemblFungi.
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;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..904
FT /note="Protein transport protein sec24"
FT /id="PRO_0000295480"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..254
FT /note="Zinc finger-like"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 904 AA; 98953 MW; 963B09A2E2F9A769 CRC64;
MAAPQGGYPP QEGYGQPAAY GSPTQQQAPT PVQHGGKKKR AYAGEAFEFG SGANAALGGQ
LPAGGSYGAY PQQQAGYQQP AAYGADPAQA YAAPAAPGVA QMTQQFGAMG MTDPHLLPPQ
PAPQAPQAPR TVPLNQLYPT DLLSQPFNVA ELDYPPPPIV LPPGTSVYPS PYANCPPKYV
RSTLNAVPTT HSLLKKSKLP FALVIQPYAA LHDSEDPIPV IPDQVISRCR RCRSYINPFV
TFLDHGHRWR CNMCNLTNDV PQAFDWDTAL QKPADRSLRP DLNHSVVEFV APQEYMVRPP
QPLVYLFLID VSYASVTNGL LATSARCIKE SLDRIPNADR RTRLGFIAVD SSLHYFSIPR
DGSENSNPQM LVVSDLDEPF LPIPGDLLVT LSECRENIES FLDKLQEMFQ NTQNNGCAMG
SALRAGYKLI APVGGKMTVL SSSLPNVGHG ALTMREDKKV LGTSKESSLL QTANSFYKSF
AVECSKAQVS VDMFLFSSQY QDVASLSNLP RYTGGQTYFY PGWNAARGED AIKFAREFSD
YLSSEIGLEA VLRVRATTGL RMNTFYGNFF NRSSDLCAFP AFPRDQAYVV EVAIDETITR
PVVCLQTAVL HTTCNGERRI RVLTLALPTT QNLADVYASA DQQAIATYFS HKAVERALGS
GLEPAREALQ SKIVELLATY RKELAGGSVS GGGLQFPANL RGLPVLFLAM IKNLGLRKSA
QIPTDMRSAA LCLLSTLPLP LLMQYIYPKM YSLHDMPDVA GLPDEKTGEI VLPPPVNLSS
ERVVPYGLYL IDDGQTQFLW VGRDAVPQLV LDVFGLPDKS QLRVGKQNLP DLDNDFNQRV
RAVVEKSRDH RSKGVGSIVV PHLYVVKEDG EPGLRLWAQT MFVEDRADQS VSLVQWMGSL
REKV
