ID SC24B_HUMAN Reviewed; 1268 AA.
AC O95487; B7ZKM8; B7ZKN4; Q0VG08;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 197.
DE RecName: Full=Protein transport protein Sec24B {ECO:0000305};
DE AltName: Full=SEC24-related protein B;
GN Name=SEC24B {ECO:0000312|HGNC:HGNC:10704};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RC TISSUE=B-cell;
RX PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
RA Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L.,
RA Paccaud J.-P.;
RT "Sec24 proteins and sorting at the endoplasmic reticulum.";
RL J. Biol. Chem. 274:7833-7840(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH SEC22B, AND MUTAGENESIS OF ARG-715.
RX PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
RA Mancias J.D., Goldberg J.;
RT "The transport signal on Sec22 for packaging into COPII-coated vesicles is
RT a conformational epitope.";
RL Mol. Cell 26:403-414(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP INTERACTION WITH RNF139.
RX PubMed=19706601; DOI=10.1074/jbc.m109.041376;
RA Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.;
RT "The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8
RT hampers ER to Golgi transport of sterol regulatory element-binding protein-
RT 2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2
RT cleavage.";
RL J. Biol. Chem. 284:28995-29004(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH TMED2 AND TMED10.
RX PubMed=20427317; DOI=10.1242/jcs.062950;
RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
RT "Selective export of human GPI-anchored proteins from the endoplasmic
RT reticulum.";
RL J. Cell Sci. 123:1705-1715(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-329 AND SER-1224, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-55 (ISOFORM 3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP INTERACTION WITH CNIH4.
RX PubMed=24405750; DOI=10.1111/tra.12148;
RA Sauvageau E., Rochdi M.D., Oueslati M., Hamdan F.F., Percherancier Y.,
RA Simpson J.C., Pepperkok R., Bouvier M.;
RT "CNIH4 interacts with newly synthesized GPCR and controls their export from
RT the endoplasmic reticulum.";
RL Traffic 15:383-400(2014).
RN [15] {ECO:0007744|PDB:3EH1}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 518-1268 IN COMPLEX WITH ZINC,
RP AND FUNCTION.
RX PubMed=18843296; DOI=10.1038/emboj.2008.208;
RA Mancias J.D., Goldberg J.;
RT "Structural basis of cargo membrane protein discrimination by the human
RT COPII coat machinery.";
RL EMBO J. 27:2918-2928(2008).
RN [16]
RP INTERACTION WITH STING1.
RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5;
RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
RA Thomsen M.K., Paludan S.R.;
RT "STEEP mediates STING ER exit and activation of signaling.";
RL Nat. Immunol. 21:868-879(2020).
RN [17]
RP ERRATUM OF PUBMED:32690950.
RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5;
RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
RA Thomsen M.K., Paludan S.R.;
RL Nat. Immunol. 21:1468-1469(2020).
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 for their transport to the Golgi complex
CC (PubMed:17499046, PubMed:20427317, PubMed:18843296). Plays a central
CC role in cargo selection within the COPII complex and together with
CC SEC24A may have a different specificity compared to SEC24C and SEC24D.
CC May package preferentially cargos with cytoplasmic DxE or LxxLE motifs
CC and may also recognize conformational epitopes (PubMed:17499046,
CC PubMed:18843296). {ECO:0000269|PubMed:17499046,
CC ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and SAR1 (PubMed:10075675,
CC PubMed:17499046). Interacts with STING1; promoting STING1 translocation
CC to COPII vesicles in a STEEP1-dependent manner (PubMed:32690950).
CC Interacts with RNF139 (PubMed:19706601). Interacts with TMED2 and
CC TMED10 (PubMed:20427317). Interacts with CNIH4 (PubMed:24405750).
CC {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:17499046,
CC ECO:0000269|PubMed:19706601, ECO:0000269|PubMed:20427317,
CC ECO:0000269|PubMed:24405750, ECO:0000269|PubMed:32690950}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000269|PubMed:10075675}; Peripheral membrane protein
CC {ECO:0000305|PubMed:10075675}; Cytoplasmic side
CC {ECO:0000305|PubMed:10075675}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10075675}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10075675}; Cytoplasmic side
CC {ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:10075675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95487-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95487-2; Sequence=VSP_035987;
CC Name=3;
CC IsoId=O95487-3; Sequence=VSP_054432, VSP_054433;
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA10335.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ131245; CAA10335.1; ALT_FRAME; mRNA.
DR EMBL; AC105314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040137; AAH40137.1; -; mRNA.
DR EMBL; BC117135; AAI17136.1; -; mRNA.
DR EMBL; BC143268; AAI43269.1; -; mRNA.
DR EMBL; BC143276; AAI43277.1; -; mRNA.
DR CCDS; CCDS43260.1; -. [O95487-2]
DR CCDS; CCDS47124.1; -. [O95487-1]
DR CCDS; CCDS75179.1; -. [O95487-3]
DR RefSeq; NP_001036199.1; NM_001042734.3. [O95487-2]
DR RefSeq; NP_001287742.1; NM_001300813.2. [O95487-3]
DR RefSeq; NP_001305014.1; NM_001318085.1.
DR RefSeq; NP_001305015.1; NM_001318086.1.
DR RefSeq; NP_006314.2; NM_006323.4. [O95487-1]
DR PDB; 3EH1; X-ray; 1.80 A; A=518-1268.
DR PDBsum; 3EH1; -.
DR AlphaFoldDB; O95487; -.
DR SMR; O95487; -.
DR BioGRID; 115696; 249.
DR ComplexPortal; CPX-2360; COPII vesicle coat complex.
DR CORUM; O95487; -.
DR IntAct; O95487; 78.
DR MINT; O95487; -.
DR STRING; 9606.ENSP00000428564; -.
DR GlyCosmos; O95487; 31 sites, 2 glycans.
DR GlyGen; O95487; 42 sites, 3 O-linked glycans (42 sites).
DR iPTMnet; O95487; -.
DR PhosphoSitePlus; O95487; -.
DR SwissPalm; O95487; -.
DR BioMuta; SEC24B; -.
DR EPD; O95487; -.
DR jPOST; O95487; -.
DR MassIVE; O95487; -.
DR MaxQB; O95487; -.
DR PaxDb; 9606-ENSP00000428564; -.
DR PeptideAtlas; O95487; -.
DR ProteomicsDB; 50915; -. [O95487-1]
DR ProteomicsDB; 50916; -. [O95487-2]
DR ProteomicsDB; 7184; -.
DR Pumba; O95487; -.
DR Antibodypedia; 48510; 56 antibodies from 13 providers.
DR DNASU; 10427; -.
DR Ensembl; ENST00000265175.5; ENSP00000265175.4; ENSG00000138802.11. [O95487-1]
DR Ensembl; ENST00000399100.6; ENSP00000382051.2; ENSG00000138802.11. [O95487-2]
DR Ensembl; ENST00000504968.6; ENSP00000428564.1; ENSG00000138802.11. [O95487-3]
DR GeneID; 10427; -.
DR KEGG; hsa:10427; -.
DR MANE-Select; ENST00000265175.5; ENSP00000265175.4; NM_006323.5; NP_006314.2.
DR UCSC; uc003hzk.4; human. [O95487-1]
DR AGR; HGNC:10704; -.
DR CTD; 10427; -.
DR DisGeNET; 10427; -.
DR GeneCards; SEC24B; -.
DR HGNC; HGNC:10704; SEC24B.
DR HPA; ENSG00000138802; Low tissue specificity.
DR MIM; 607184; gene.
DR neXtProt; NX_O95487; -.
DR OpenTargets; ENSG00000138802; -.
DR PharmGKB; PA35627; -.
DR VEuPathDB; HostDB:ENSG00000138802; -.
DR eggNOG; KOG1985; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_2_0_1; -.
DR InParanoid; O95487; -.
DR OMA; CAHYAMS; -.
DR OrthoDB; 977017at2759; -.
DR PhylomeDB; O95487; -.
DR TreeFam; TF354244; -.
DR PathwayCommons; O95487; -.
DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; O95487; -.
DR SIGNOR; O95487; -.
DR BioGRID-ORCS; 10427; 20 hits in 1155 CRISPR screens.
DR ChiTaRS; SEC24B; human.
DR EvolutionaryTrace; O95487; -.
DR GeneWiki; SEC24B; -.
DR GenomeRNAi; 10427; -.
DR Pharos; O95487; Tbio.
DR PRO; PR:O95487; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O95487; Protein.
DR Bgee; ENSG00000138802; Expressed in cartilage tissue and 217 other cell types or tissues.
DR Genevisible; O95487; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; IEA:Ensembl.
DR GO; GO:1901301; P:regulation of cargo loading into COPII-coated vesicle; IEA:Ensembl.
DR GO; GO:0090178; P:regulation of establishment of planar polarity involved in neural tube closure; IEA:Ensembl.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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 PANTHER; PTHR13803:SF42; PROTEIN TRANSPORT PROTEIN SEC24B; 1.
DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
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; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1268
FT /note="Protein transport protein Sec24B"
FT /id="PRO_0000205155"
FT REPEAT 1141..1213
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..629
FT /note="Zinc finger-like"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..451
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH1"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH1"
FT BINDING 626
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH1"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH1"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 44
FT /note="N -> NETGFHHVAQASLELLDPSNLPASASQIAGST (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054432"
FT VAR_SEQ 354..388
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035987"
FT VAR_SEQ 496
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054433"
FT VARIANT 456
FT /note="A -> G (in dbSNP:rs35705351)"
FT /id="VAR_047934"
FT MUTAGEN 715
FT /note="R->A: Decreased ability to package the SNARE SEC22B
FT cargo into COPII vesicles. Has no effect on other cargos
FT packaging."
FT /evidence="ECO:0000269|PubMed:17499046"
FT CONFLICT 23
FT /note="A -> S (in Ref. 1; CAA10335)"
FT /evidence="ECO:0000305"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 548..553
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 560..570
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 617..625
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 668..670
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 688..693
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 695..706
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 707..709
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 717..731
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 740..745
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 762..765
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 766..775
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 790..801
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 802..804
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 806..812
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 831..834
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 847..857
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 860..866
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 874..877
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 879..882
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 896..898
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 900..915
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 919..928
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 932..943
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 945..954
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 960..968
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 974..985
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 991..1003
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1006..1011
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1015..1032
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1035..1054
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1066..1068
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1069..1071
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1074..1082
FT /evidence="ECO:0007829|PDB:3EH1"
FT TURN 1085..1087
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1095..1107
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1110..1117
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1120..1123
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1138..1140
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1150..1152
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1157..1162
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1164..1171
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1177..1182
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1189..1191
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1194..1196
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1205..1219
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1221..1223
FT /evidence="ECO:0007829|PDB:3EH1"
FT STRAND 1226..1236
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1237..1241
FT /evidence="ECO:0007829|PDB:3EH1"
FT HELIX 1255..1267
FT /evidence="ECO:0007829|PDB:3EH1"
FT MOD_RES O95487-3:55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1268 AA; 137418 MW; 0E08B982D0982F84 CRC64;
MSAPAGSSHP AASARIPPKF GGAAVSGAAA PAGPGAGPAP HQQNGPAQNQ MQVPSGYGLH
HQNYIAPSGH YSQGPGKMTS LPLDTQCGDY YSALYTVPTQ NVTPNTVNQQ PGAQQLYSRG
PPAPHIVGST LGSFQGAASS ASHLHTSASQ PYSSFVNHYN SPAMYSASSS VASQGFPSTC
GHYAMSTVSN AAYPSVSYPS LPAGDTYGQM FTSQNAPTVR PVKDNSFSGQ NTAISHPSPL
PPLPSQQHHQ QQSLSGYSTL TWSSPGLPST QDNLIRNHTG SLAVANNNPT ITVADSLSCP
VMQNVQPPKS SPVVSTVLSG SSGSSSTRTP PTANHPVEPV TSVTQPSELL QQKGVQYGEY
VNNQASSAPT PLSSTSDDEE EEEEDEEAGV DSSSTTSSAS PMPNSYDALE GGSYPDMLSS
SASSPAPDPA PEPDPASAPA PASAPAPVVP QPSKMAKPFG YGYPTLQPGY QNATAPLISG
VQPSNPVYSG FQQYPQQYPG VNQLSSSIGG LSLQSSPQPE SLRPVNLTQE RNILPMTPVW
APVPNLNADL KKLNCSPDSF RCTLTNIPQT QALLNKAKLP LGLLLHPFRD LTQLPVITSN
TIVRCRSCRT YINPFVSFID QRRWKCNLCY RVNDVPEEFM YNPLTRSYGE PHKRPEVQNS
TVEFIASSDY MLRPPQPAVY LFVLDVSHNA VEAGYLTILC QSLLENLDKL PGDSRTRIGF
MTFDSTIHFY NLQEGLSQPQ MLIVSDIDDV FLPTPDSLLV NLYESKELIK DLLNALPNMF
TNTRETHSAL GPALQAAFKL MSPTGGRVSV FQTQLPSLGA GLLQSREDPN QRSSTKVVQH
LGPATDFYKK LALDCSGQQT AVDLFLLSSQ YSDLASLACM SKYSAGCIYY YPSFHYTHNP
SQAEKLQKDL KRYLTRKIGF EAVMRIRCTK GLSMHTFHGN FFVRSTDLLS LANINPDAGF
AVQLSIEESL TDTSLVCFQT ALLYTSSKGE RRIRVHTLCL PVVSSLADVY AGVDVQAAIC
LLANMAVDRS VSSSLSDARD ALVNAVVDSL SAYGSTVSNL QHSALMAPSS LKLFPLYVLA
LLKQKAFRTG TSTRLDDRVY AMCQIKSQPL VHLMKMIHPN LYRIDRLTDE GAVHVNDRIV
PQPPLQKLSA EKLTREGAFL MDCGSVFYIW VGKGCDNNFI EDVLGYTNFA SIPQKMTHLP
ELDTLSSERA RSFITWLRDS RPLSPILHIV KDESPAKAEF FQHLIEDRTE AAFSYYEFLL
HVQQQICK
//
