SC23B_HUMAN
ID SC23B_HUMAN Reviewed; 767 AA.
AC Q15437; D3DW33; Q503A9; Q5W183; Q9BS15; Q9BSI2; Q9H1D7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein transport protein Sec23B {ECO:0000305};
DE Short=hSec23B {ECO:0000303|PubMed:8898360};
DE AltName: Full=SEC23-related protein B;
GN Name=SEC23B {ECO:0000312|HGNC:HGNC:10702};
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], VARIANT GLN-489, AND TISSUE SPECIFICITY.
RC TISSUE=B-cell;
RX PubMed=8898360; DOI=10.1091/mbc.7.10.1535;
RA Paccaud J.-P., Reith W., Carpentier J.-L., Ravazzola M., Amherdt M.,
RA Schekman R., Orci L.;
RT "Cloning and functional characterization of mammalian homologues of the
RT COPII component Sec23.";
RL Mol. Biol. Cell 7:1535-1546(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-373 AND LEU-433.
RC TISSUE=Cervix, Placenta, and Uterus;
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP IDENTIFICATION BY MASS 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 [9]
RP VARIANTS CDAN2 TRP-14; LYS-109; ALA-348; CYS-497; LEU-603 AND CYS-701, AND
RP VARIANT GLN-489.
RX PubMed=19621418; DOI=10.1002/humu.21077;
RA Bianchi P., Fermo E., Vercellati C., Boschetti C., Barcellini W., Iurlo A.,
RA Marcello A.P., Righetti P.G., Zanella A.;
RT "Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations
RT in the SEC23B gene.";
RL Hum. Mutat. 30:1292-1298(2009).
RN [10]
RP VARIANTS CDAN2 TRP-14; LYS-109 AND TRP-530, VARIANTS HIS-18; GLY-239;
RP HIS-313; THR-318; ARG-386; ILE-426; CYS-462; CYS-497 AND VAL-524,
RP CHARACTERIZATION OF VARIANTS CDAN2 TRP-14 AND LYS-109, AND CHARACTERIZATION
RP OF VARIANT GLY-239.
RX PubMed=19561605; DOI=10.1038/ng.405;
RA Schwarz K., Iolascon A., Verissimo F., Trede N.S., Horsley W., Chen W.,
RA Paw B.H., Hopfner K.-P., Holzmann K., Russo R., Esposito M.R., Spano D.,
RA De Falco L., Heinrich K., Joggerst B., Rojewski M.T., Perrotta S.,
RA Denecke J., Pannicke U., Delaunay J., Pepperkok R., Heimpel H.;
RT "Mutations affecting the secretory COPII coat component SEC23B cause
RT congenital dyserythropoietic anemia type II.";
RL Nat. Genet. 41:936-940(2009).
RN [11]
RP VARIANTS CWS7 LEU-164 AND GLY-594, CHARACTERIZATION OF VARIANT CWS7
RP GLY-594, INTERACTION WITH SAR1A, AND SUBCELLULAR LOCATION.
RX PubMed=26522472; DOI=10.1016/j.ajhg.2015.10.001;
RA Yehia L., Niazi F., Ni Y., Ngeow J., Sankunny M., Liu Z., Wei W.,
RA Mester J.L., Keri R.A., Zhang B., Eng C.;
RT "Germline heterozygous variants in SEC23B are associated with Cowden
RT syndrome and enriched in apparently sporadic thyroid cancer.";
RL Am. J. Hum. Genet. 97:661-676(2015).
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 {ECO:0000250|UniProtKB:Q15436}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1 (By similarity). Interacts with
CC SAR1A (PubMed:26522472). {ECO:0000250|UniProtKB:Q15436,
CC ECO:0000269|PubMed:26522472}.
CC -!- INTERACTION:
CC Q15437; Q8N684: CPSF7; NbExp=3; IntAct=EBI-742673, EBI-746909;
CC Q15437; Q86UW9: DTX2; NbExp=6; IntAct=EBI-742673, EBI-740376;
CC Q15437; Q969F0: FATE1; NbExp=3; IntAct=EBI-742673, EBI-743099;
CC Q15437; O43365: HOXA3; NbExp=4; IntAct=EBI-742673, EBI-8643838;
CC Q15437; P42858: HTT; NbExp=3; IntAct=EBI-742673, EBI-466029;
CC Q15437; Q96M27: PRRC1; NbExp=3; IntAct=EBI-742673, EBI-2560879;
CC Q15437; Q13671: RIN1; NbExp=3; IntAct=EBI-742673, EBI-366017;
CC Q15437; Q15436: SEC23A; NbExp=3; IntAct=EBI-742673, EBI-81088;
CC Q15437; O94855: SEC24D; NbExp=6; IntAct=EBI-742673, EBI-748817;
CC Q15437; O94855-2: SEC24D; NbExp=3; IntAct=EBI-742673, EBI-12081096;
CC Q15437; P09234: SNRPC; NbExp=3; IntAct=EBI-742673, EBI-766589;
CC Q15437; Q8N205: SYNE4; NbExp=3; IntAct=EBI-742673, EBI-7131783;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26522472}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15436}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:8898360}.
CC -!- DISEASE: Cowden syndrome 7 (CWS7) [MIM:616858]: A form of Cowden
CC syndrome, a hamartomatous polyposis syndrome with age-related
CC penetrance. Cowden syndrome is characterized by hamartomatous lesions
CC affecting derivatives of ectodermal, mesodermal and endodermal layers,
CC macrocephaly, facial trichilemmomas (benign tumors of the hair follicle
CC infundibulum), acral keratoses, papillomatous papules, and elevated
CC risk for development of several types of malignancy, particularly
CC breast carcinoma in women and thyroid carcinoma in both men and women.
CC Colon cancer and renal cell carcinoma have also been reported.
CC Hamartomas can be found in virtually every organ, but most commonly in
CC the skin, gastrointestinal tract, breast and thyroid. CWS7 inheritance
CC is autosomal dominant. {ECO:0000269|PubMed:26522472}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Anemia, congenital dyserythropoietic, 2 (CDAN2) [MIM:224100]:
CC An autosomal recessive blood disorder characterized by morphological
CC abnormalities of erythroblasts, ineffective erythropoiesis, normocytic
CC anemia, iron overload, jaundice, and variable splenomegaly.
CC Ultrastructural features include bi- or multinucleated erythroblasts in
CC bone marrow, karyorrhexis, and the presence of Gaucher-like bone marrow
CC histiocytes. The main biochemical feature of the disease is defective
CC glycosylation of some red blood cells membrane proteins.
CC {ECO:0000269|PubMed:19561605, ECO:0000269|PubMed:19621418}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000305}.
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DR EMBL; X97065; CAA65775.1; -; mRNA.
DR EMBL; AL121893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10231.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10232.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10233.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10234.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10235.1; -; Genomic_DNA.
DR EMBL; BC005032; AAH05032.1; -; mRNA.
DR EMBL; BC005404; AAH05404.1; -; mRNA.
DR EMBL; BC095404; AAH95404.1; -; mRNA.
DR CCDS; CCDS13137.1; -.
DR RefSeq; NP_001166216.1; NM_001172745.1.
DR RefSeq; NP_006354.2; NM_006363.4.
DR RefSeq; NP_116780.1; NM_032985.4.
DR RefSeq; NP_116781.1; NM_032986.3.
DR RefSeq; XP_016883082.1; XM_017027593.1.
DR AlphaFoldDB; Q15437; -.
DR SMR; Q15437; -.
DR BioGRID; 115746; 174.
DR IntAct; Q15437; 46.
DR MINT; Q15437; -.
DR STRING; 9606.ENSP00000338844; -.
DR GlyGen; Q15437; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15437; -.
DR MetOSite; Q15437; -.
DR PhosphoSitePlus; Q15437; -.
DR BioMuta; SEC23B; -.
DR DMDM; 20141794; -.
DR EPD; Q15437; -.
DR jPOST; Q15437; -.
DR MassIVE; Q15437; -.
DR MaxQB; Q15437; -.
DR PaxDb; Q15437; -.
DR PeptideAtlas; Q15437; -.
DR PRIDE; Q15437; -.
DR ProteomicsDB; 60596; -.
DR Antibodypedia; 1407; 197 antibodies from 23 providers.
DR DNASU; 10483; -.
DR Ensembl; ENST00000262544.6; ENSP00000262544.2; ENSG00000101310.17.
DR Ensembl; ENST00000336714.8; ENSP00000338844.3; ENSG00000101310.17.
DR Ensembl; ENST00000377465.6; ENSP00000366685.1; ENSG00000101310.17.
DR Ensembl; ENST00000650089.1; ENSP00000497473.1; ENSG00000101310.17.
DR GeneID; 10483; -.
DR KEGG; hsa:10483; -.
DR MANE-Select; ENST00000650089.1; ENSP00000497473.1; NM_006363.6; NP_006354.2.
DR UCSC; uc002wqz.3; human.
DR CTD; 10483; -.
DR DisGeNET; 10483; -.
DR GeneCards; SEC23B; -.
DR HGNC; HGNC:10702; SEC23B.
DR HPA; ENSG00000101310; Low tissue specificity.
DR MalaCards; SEC23B; -.
DR MIM; 224100; phenotype.
DR MIM; 610512; gene.
DR MIM; 616858; phenotype.
DR neXtProt; NX_Q15437; -.
DR OpenTargets; ENSG00000101310; -.
DR Orphanet; 98873; Congenital dyserythropoietic anemia type II.
DR Orphanet; 201; Cowden syndrome.
DR PharmGKB; PA35625; -.
DR VEuPathDB; HostDB:ENSG00000101310; -.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q15437; -.
DR OMA; TSRIWFC; -.
DR OrthoDB; 270617at2759; -.
DR PhylomeDB; Q15437; -.
DR TreeFam; TF300693; -.
DR PathwayCommons; Q15437; -.
DR SignaLink; Q15437; -.
DR SIGNOR; Q15437; -.
DR BioGRID-ORCS; 10483; 42 hits in 1079 CRISPR screens.
DR ChiTaRS; SEC23B; human.
DR GeneWiki; SEC23B; -.
DR GenomeRNAi; 10483; -.
DR Pharos; Q15437; Tbio.
DR PRO; PR:Q15437; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q15437; protein.
DR Bgee; ENSG00000101310; Expressed in endothelial cell and 193 other tissues.
DR ExpressionAtlas; Q15437; baseline and differential.
DR Genevisible; Q15437; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; cd11287; Sec23_C; 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; IPR037364; Sec23.
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; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PTHR11141; 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; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
PE 1: Evidence at protein level;
KW Acetylation; Congenital dyserythropoietic anemia; Cytoplasm;
KW Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum;
KW ER-Golgi transport; Hereditary hemolytic anemia; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..767
FT /note="Protein transport protein Sec23B"
FT /id="PRO_0000205148"
FT REPEAT 634..720
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 564
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D662"
FT VARIANT 14
FT /note="R -> W (in CDAN2; the mutant protein is unstable
FT with less than 5% of protein detectable compared to wild-
FT type; dbSNP:rs121918222)"
FT /evidence="ECO:0000269|PubMed:19561605,
FT ECO:0000269|PubMed:19621418"
FT /id="VAR_062294"
FT VARIANT 18
FT /note="R -> H (in dbSNP:rs905074313)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062295"
FT VARIANT 109
FT /note="E -> K (in CDAN2; the mutant protein is unstable
FT with less than 5% of protein detectable compared to wild-
FT type; dbSNP:rs121918221)"
FT /evidence="ECO:0000269|PubMed:19561605,
FT ECO:0000269|PubMed:19621418"
FT /id="VAR_062296"
FT VARIANT 164
FT /note="V -> L (in CWS7; unknown pathological significance;
FT dbSNP:rs36023150)"
FT /evidence="ECO:0000269|PubMed:26522472"
FT /id="VAR_076424"
FT VARIANT 239
FT /note="D -> G (the mutant protein is expressed as the wild-
FT type; dbSNP:rs761034212)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062297"
FT VARIANT 313
FT /note="R -> H (in dbSNP:rs750888081)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062298"
FT VARIANT 318
FT /note="I -> T (in dbSNP:rs953079477)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062299"
FT VARIANT 348
FT /note="D -> A (in CDAN2)"
FT /evidence="ECO:0000269|PubMed:19621418"
FT /id="VAR_062300"
FT VARIANT 373
FT /note="M -> V (in dbSNP:rs17849992)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_062301"
FT VARIANT 386
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062302"
FT VARIANT 426
FT /note="V -> I (in dbSNP:rs41309927)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062303"
FT VARIANT 433
FT /note="P -> L (in dbSNP:rs17807673)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034482"
FT VARIANT 462
FT /note="Y -> C (in dbSNP:rs780978419)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062304"
FT VARIANT 489
FT /note="H -> Q (in dbSNP:rs2273526)"
FT /evidence="ECO:0000269|PubMed:19621418,
FT ECO:0000269|PubMed:8898360"
FT /id="VAR_020318"
FT VARIANT 497
FT /note="R -> C (in CDAN2; unknown pathological significance;
FT dbSNP:rs727504145)"
FT /evidence="ECO:0000269|PubMed:19561605,
FT ECO:0000269|PubMed:19621418"
FT /id="VAR_062305"
FT VARIANT 524
FT /note="A -> V (in dbSNP:rs398124225)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062306"
FT VARIANT 530
FT /note="R -> W (in CDAN2; dbSNP:rs121918223)"
FT /evidence="ECO:0000269|PubMed:19561605"
FT /id="VAR_062307"
FT VARIANT 594
FT /note="V -> G (in CWS7; aberrant aggregation; causes
FT mislocalization of the protein in the cytoplasm; reduces
FT interaction with SAR1A; confers endoplasmic reticulum (ER)
FT stress-mediated cell growth advantage; dbSNP:rs752366963)"
FT /evidence="ECO:0000269|PubMed:26522472"
FT /id="VAR_076425"
FT VARIANT 603
FT /note="S -> L (in CDAN2)"
FT /evidence="ECO:0000269|PubMed:19621418"
FT /id="VAR_062308"
FT VARIANT 701
FT /note="R -> C (in CDAN2; dbSNP:rs201270568)"
FT /evidence="ECO:0000269|PubMed:19621418"
FT /id="VAR_062309"
SQ SEQUENCE 767 AA; 86479 MW; 1A00DE39D56B0204 CRC64;
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLKERPD LPPVQYEPVL
CSRPTCKAVL NPLCQVDYRA KLWACNFCFQ RNQFPPAYGG ISEVNQPAEL MPQFSTIEYV
IQRGAQSPLI FLYVVDTCLE EDDLQALKES LQMSLSLLPP DALVGLITFG RMVQVHELSC
EGISKSYVFR GTKDLTAKQI QDMLGLTKPA MPMQQARPAQ PQEHPFASSR FLQPVHKIDM
NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP
GMVVGDELKI PIRSWHDIEK DNARFMKKAT KHYEMLANRT AANGHCIDIY ACALDQTGLL
EMKCCANLTG GYMVMGDSFN TSLFKQTFQR IFTKDFNGDF RMAFGATLDV KTSRELKIAG
AIGPCVSLNV KGPCVSENEL GVGGTSQWKI CGLDPTSTLG IYFEVVNQHN TPIPQGGRGA
IQFVTHYQHS STQRRIRVTT IARNWADVQS QLRHIEAAFD QEAAAVLMAR LGVFRAESEE
GPDVLRWLDR QLIRLCQKFG QYNKEDPTSF RLSDSFSLYP QFMFHLRRSP FLQVFNNSPD
ESSYYRHHFA RQDLTQSLIM IQPILYSYSF HGPPEPVLLD SSSILADRIL LMDTFFQIVI
YLGETIAQWR KAGYQDMPEY ENFKHLLQAP LDDAQEILQA RFPMPRYINT EHGGSQARFL
LSKVNPSQTH NNLYAWGQET GAPILTDDVS LQVFMDHLKK LAVSSAC
