SEC24_USTMA
ID SEC24_USTMA Reviewed; 995 AA.
AC Q4P9K4; A0A0D1E238;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; ORFNames=UMAG_03209;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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; CM003147; KIS68635.1; -; Genomic_DNA.
DR RefSeq; XP_011389645.1; XM_011391343.1.
DR AlphaFoldDB; Q4P9K4; -.
DR SMR; Q4P9K4; -.
DR STRING; 5270.UM03209P0; -.
DR EnsemblFungi; KIS68635; KIS68635; UMAG_03209.
DR GeneID; 23563733; -.
DR KEGG; uma:UMAG_03209; -.
DR VEuPathDB; FungiDB:UMAG_03209; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q4P9K4; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000000561; Chromosome 8.
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 CDD; cd00201; WW; 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; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_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; PF00397; WW; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 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..995
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295503"
FT DOMAIN 6..40
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 25..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..348
FT /note="Zinc finger-like"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 995 AA; 106974 MW; 51E3A335CD893EBD CRC64;
MAQPPPQLPP GWVAQWDPNA ARQVFVETAT GRTSWQPPTA GPAGVAPPQQ HQQRPTHPQG
QARMSMPQIQ PPPGMRGPSL SPISQHGPGA PVSPPSAGSP APASIGPGAS RRRAYPTAHL
AANSISYAGG YDASTATGAG VAYPGAQDAQ PQLFTPGAPD LTPSPYGAAA QPALGAPGLA
PAPGAHGAPG VGPAPGYAAG GVQGITNQFQ AMGVGGGVAG GMGQKFSTLQ TVNISGVQPN
VNDLERPPPE IRLPPNACVS TNPKANADPS YQRCTLNAVP TTSSLLQKSK IPLGLILSPY
RSVREADGDE PVPVVTDTVI ARCRRCRTYI NPYVTFIENG NRWKCCMCNI SNEVPQLFDW
NSETNQPADR WQRPELNHSV VEFIAPREYM VRPPQPPVYT FLIDVSYQAV NSGMVATAAR
TILETLDRLP NSDNRAKICI IGVDTSLHFF SITPEGTEPD MLVVSDLDDV FLPKPNDLLV
NLTECRAGVE ALLQRLGDMY KDSLVTGSAL GAALQAAYKL ISPIGGKIMV LTASLPSVGP
GALKNREDPK LLGTAKESTL LGAASSFYKT FPIDCSRSQV SVDMFLFAPS YTDVATLSCL
PRYTGGQTFF YPAFHAGRAE DAVKFSHEFS EVLASPISYE AVLRLRATKG IRATAFHGNF
FVRSTDLLAL PSVPLDQNYA IECEIEETIN APFVVFQSVV LHSTSSGERR IRVINLALPT
TSSMSEVYAN ADQIAIATLL ADKAVERSIH SRLEDARDAL FNKLVDVFST YKSTMTSAGS
GASPQLAIAQ NLAQLPLLVL ALLKHVGIRQ SSSIPSDLRA YAQALLTTLP AQQLIPYLHA
SFYCLHNMAP EAGTTVAEKG FVMPAKLNLT SERFERHGLY LIEDGQNIFL WVGREAVPQL
CLDVFDVANY GTLRGGKTTL PKLDNSMNQR VNAIVQRIRD SRRGPYRPHL YIVKEDGEPS
LRLWALSLLI EDRFEQSPSY MQFIGQLRDK VNGGS
