SEC24_PODAS
ID SEC24_PODAS Reviewed; 946 AA.
AC Q86ZK8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; ORFNames=Pa5D0034;
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s;
RX PubMed=12892638; DOI=10.1016/s1087-1845(03)00025-2;
RA Silar P., Barreau C., Debuchy R., Kicka S., Turcq B., Sainsard-Chanet A.,
RA Sellem C.H., Billault A., Cattolico L., Duprat S., Weissenbach J.;
RT "Characterization of the genomic organization of the region bordering the
RT centromere of chromosome V of Podospora anserina by direct sequencing.";
RL Fungal Genet. Biol. 39:250-263(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; BX088700; CAD60721.1; -; Genomic_DNA.
DR AlphaFoldDB; Q86ZK8; -.
DR SMR; Q86ZK8; -.
DR VEuPathDB; FungiDB:PODANS_5_5670; -.
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..946
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295497"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..295
FT /note="Zinc finger-like"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 946 AA; 103032 MW; 00D974A33B702874 CRC64;
MSGASNDGYG QYPPQQPGDH QQQPPYPDQA YDNAAPVAPG HAADHGRKKK RQYAASAFDV
GVGGNVVAGG QPIPGAAPYG APAAVPAYGG YPAQPEVQPA AYGAQPAQPY GQPAAVSGYQ
APDPYYPSAG AVPAPGGVAG LTAGFQGMNL GAGAPGGIPQ QQPQQLPPQA RAGPLNQLYP
TDLLNQPFNV SELDLPPPPI ILPPNASVTP SPDANCLPKY VRSTLNAVPT THSLLKKSKL
PFSLVIQPYA ALHDLDDPVP VVQDQVISRC RRCRSYINPF VTFLDHGHRW RCNMCNLTND
VPQAFDWDAA AQKSVDRWQR HELNHAVVEF VAPQEYMVRP PQPLVYLFLF DVSYASVSSG
LLATAARTIE ASLDRIPNAD RRTRLGFMAV DSSLHYFSVP KDTDENGETS MLVVSDLDEP
FLPVPGELLV PLTESRRSIE NFLTKLPKMF EHNQDNGSCM GSALRAGDKL ISPLGGKLVV
LSASLPNVGH GKLTMREDKK LLGTSKEGSL LQTAATFYKS FAVECSKNQV SIDMFLFSSQ
YQDVASLSNL PRYTGGQTWF YPGWNAGRAE DAIKFASEFR DYLSSEIGLE AVLRVRATTG
LRMSTFYGNF FTRSSDLCAF PAFPRDQCYV VEVAIDENLT KDVVCMQTAV LHTTCNGERR
IRVMTLALPT TTNLADVYAS ADQAAITTYY THKAVERALG SGLDSARDLL QKTITDLLQT
FKKELAGGSM GGGLQFPSNL RGLPALFLGL MKHVGLRKSA QIPSDLRSAA LCLLSTLPVP
LLMQYIYPRL YSLHDMPDNA GIPDPETSQI VLPPPLNLSS EKFVPYGLYL IDDGQTQFLW
VGREAVPQLL VDVFDVADRT QLQVGKATLK ELDNDFNERV RAVIQKSRDH KSKGVGSIIV
PHLYIVREDG EPSLKLWAQT LLVEDRADQG LSYVQWMGSL REKVSS
