SC24B_ARATH
ID SC24B_ARATH Reviewed; 1080 AA.
AC Q9M081; F4JV31; O65535;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Protein transport protein Sec24-like At4g32640;
GN OrderedLocusNames=At4g32640; ORFNames=F4D11.160;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Component of the COPII coat, that covers ER-derived vesicles
CC involved in transport from the endoplasmic reticulum to the Golgi
CC apparatus. COPII is composed of at least five proteins: the SEC23/24
CC complex, the SEC13/31 complex, and the protein SAR1. Acts in the
CC cytoplasm to promote the transport of secretory, plasma membrane, and
CC vacuolar proteins from the endoplasmic reticulum to the Golgi complex
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95486}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95486}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18597.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79981.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022537; CAA18597.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161581; CAB79981.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86094.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86095.1; -; Genomic_DNA.
DR PIR; D85383; D85383.
DR RefSeq; NP_001119101.5; NM_001125629.5.
DR RefSeq; NP_194990.5; NM_119416.8.
DR AlphaFoldDB; Q9M081; -.
DR SMR; Q9M081; -.
DR BioGRID; 14685; 6.
DR STRING; 3702.AT4G32640.2; -.
DR iPTMnet; Q9M081; -.
DR PaxDb; Q9M081; -.
DR PRIDE; Q9M081; -.
DR ProteomicsDB; 232933; -.
DR EnsemblPlants; AT4G32640.1; AT4G32640.1; AT4G32640.
DR EnsemblPlants; AT4G32640.2; AT4G32640.2; AT4G32640.
DR GeneID; 829399; -.
DR Gramene; AT4G32640.1; AT4G32640.1; AT4G32640.
DR Gramene; AT4G32640.2; AT4G32640.2; AT4G32640.
DR KEGG; ath:AT4G32640; -.
DR Araport; AT4G32640; -.
DR eggNOG; KOG1984; Eukaryota.
DR HOGENOM; CLU_004589_4_0_1; -.
DR InParanoid; Q9M081; -.
DR OMA; DRRVHDM; -.
DR OrthoDB; 330236at2759; -.
DR PRO; PR:Q9M081; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M081; baseline and differential.
DR Genevisible; Q9M081; AT.
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; 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; 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 Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1080
FT /note="Protein transport protein Sec24-like At4g32640"
FT /id="PRO_0000205159"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..455
FT /note="Zinc finger-like"
FT COMPBIAS 15..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 116322 MW; 0F70081A33F4F431 CRC64;
MVAPVPPGAP RPNSQQNSGP PNFYPGSQGN SNALADNMQN LSLNRPPPMM PGSGPRPPPP
FGQSPQPFPQ QSPSYGAPQR GPSPMSRPGP PAGMARPGGP PPVSQPAGFQ SNVPLNRPTG
PPSRQPSFGS RPSMPGGPVA QPAASSSGFP AFGPSGSVAA GPPPGSRPMA FGSPPPVGSG
MSMPPSGMIG GPVSNGHQMV GSGGFPRGTQ FPGAAVTTPQ APYVRPPSAP YARTPPQPLG
SHSLSGNPPL TPFTAPSMPP PATFPGAPHG RPAVSGLPYG PPSAQVAPPL GFPGQMQPPR
YGMGPLPNQS MTNIPTAMGQ PGATVPGPSR IDPNQIPRPG SSSSPTVFET RQSNQANPPP
PATSDYVVRD TGNCSPRYMR CTINQIPCTV DLLSTSGMQL ALMVQPLALS HPSEEPIQVV
DFGEGGPVRC SRCKGYINPF MKFIDQGRKF ICNFCGYTDE TPRDYHCNLG PDGRRRDVDE
RPELCRGTVE FVATKEYMVR DPMPAVYFFL IDVSMNAIQT GATAAACNAI QQVLSDLPEG
PRTFVGIATF DSTIHFYNLK RALQQPLMLI VPDVQDVYTP LETDVVVQLS ECRQHLELLL
DSIPTMFQES KIPESAFGAA VKAAFLAMKS KGGKLMVFQS ILCSVGVGAL SSREAEGRAN
MSAGEKEAHK LLQPADKTLK TMAIEFAEYQ VCVDIFITTQ AYVDMASISV IPRTTGGQVY
CYYPFSALSD PPKLYNDLKW NITRPQGFEA VMRVRCSQGI QVQEYSGNFC KRIPTDIDLP
AHDDKLQDGA ECAFQCALLY TTIYGERRIR VTTLSLSCTN MLSNLFRAAD LDSQFACMLK
QAANEIPSKA LPLVKEQATN SCINALYAYR KFCATVTSSG QLILPEALKL FPLYTLALTK
SVGLRTDGRI DDRSFWINYV SSLSTPLAIP LVYPRMISVH DLDVKDTEGS VLPPPIPLSS
EHISNEGVYF LENGEDGLLF VGESVDSDIL QKLFAVSSAA EIPNQFVLQQ YDNQLSKKFN
DAVNEIRRQR CSYLRIKLCK KGEPSGMLFL SYMVEDRTAS GPSYVEFLVQ VHRQIQLKMN
