SEC24_NEUCR
ID SEC24_NEUCR Reviewed; 950 AA.
AC Q7S4P3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein transport protein sec24;
GN Name=sec24; ORFNames=NCU02391;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(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 vtr-7/sar1.
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; CM002242; EAA30475.1; -; Genomic_DNA.
DR RefSeq; XP_959711.1; XM_954618.2.
DR AlphaFoldDB; Q7S4P3; -.
DR SMR; Q7S4P3; -.
DR STRING; 5141.EFNCRP00000003187; -.
DR EnsemblFungi; EAA30475; EAA30475; NCU02391.
DR GeneID; 3875858; -.
DR KEGG; ncr:NCU02391; -.
DR VEuPathDB; FungiDB:NCU02391; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q7S4P3; -.
DR OMA; TFPRDQS; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
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:0000139; C:Golgi 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; IBA:GO_Central.
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..950
FT /note="Protein transport protein sec24"
FT /id="PRO_0000295493"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..299
FT /note="Zinc finger-like"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 950 AA; 103531 MW; 08363F52A4F28E9C CRC64;
MAAPPPNDGY GQYPPQQYGE QPQYPVEPAQ QAYGSPASPP PAAASQHGAE HGKKKKRAYA
AQAFEVATGG NAVVGGQPAA TQYGIPQPAA PGFGGYPAQD AQQVAYGAPT TPYGAPQPAV
PGVGGYQAPD PYYSQGVPPA AVGPAPGGVA GITAGIQSMG FGGQPQQPQQ LPAQTRGLVN
QLYPTDLLNQ PFNVAELELP PPPIILPPNS SVTPSPDANC APKYVRSTLN AVPTTHSLLK
KSKLPFALVI QPYAALHDLD DPVPVVQDQV ISRCRRCRSY INPFVTFLDH GHRWRCNMCN
LTNDVPQAFD WDAAAQKSVD RWQRPELNHA VVEFVAPQEY MVRPPQPLVY LFLFDVSYAA
VSTGLLATSA RTILDSLDRI PNADRRTRLG FIAVDSSLHY FSVPRDTEEN GETSMLVVSD
LDEPFLPVPG ELLVPLTECR QNIESFLNKL PEMFANNQSN GNCMGSALRA GHKLIAPLGG
KIVVLSSSLP NVGYGKLEMR EDKKLLGTSK ESGLLQTANS FYKSFAVECS KNQVSIDMFL
FSSQYQDVAS LSNLPRYTGG QTWFYPGWNA ARAEDAVKFA SEFSDYLSSE IGLEAVLRVR
ATTGLRMSTF YGNFFNRSSD LCAFPAFPRD QCYVVEVAID ENLTKNFVCL QTAVLHTTCN
GERRIRVMTL ALPTTTNLAD VYASADQCAI ATYFSHKAVE KALGNSLDAA RDLPQQKLTE
LLQTFRKELG GGSMGGGLQF PSNLRGLPAL CLGLTKHVGL RKSALIPSDI RSAALCQLST
LPLPLLMQYI YPRLYSLHDM PDNAGIPDPE TSQIVLPPPM NLSSERFVPF GLYLIDDGQT
QFLWVGRDAV PQLILDVFGV QERTQVAVGK GTLPELDNDF NERVRNVIAK SRDHKSKGVG
SITLPHLYIV REDGEPSLKL WAQTLLVEDR ADQGMSFQQW MGMLREKVVQ
