Protein transport protein Sec23B (hSec23B) (SEC23-related protein B)

 SC23B_HUMAN             Reviewed;         767 AA.
 Q15437; D3DW33; Q503A9; Q5W183; Q9BS15; Q9BSI2; Q9H1D7;
 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
 23-JAN-2002, sequence version 2.
 07-APR-2021, entry version 189.
 RecName: Full=Protein transport protein Sec23B {ECO:0000305};
          Short=hSec23B {ECO:0000303|PubMed:8898360};
 AltName: Full=SEC23-related protein B;
 Name=SEC23B {ECO:0000312|HGNC:HGNC:10702};
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
 Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-489, AND TISSUE SPECIFICITY.
 TISSUE=B-cell;
 PubMed=8898360; DOI=10.1091/mbc.7.10.1535;
 Paccaud J.-P., Reith W., Carpentier J.-L., Ravazzola M., Amherdt M.,
 Schekman R., Orci L.;
 "Cloning and functional characterization of mammalian homologues of the
 COPII component Sec23.";
 Mol. Biol. Cell 7:1535-1546(1996).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=11780052; DOI=10.1038/414865a;
 Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
 Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
 Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
 Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
 Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
 Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
 Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
 Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
 Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
 Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
 Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
 Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
 Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
 Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
 Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
 Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
 Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
 Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
 Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
 Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
 Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
 Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
 Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
 "The DNA sequence and comparative analysis of human chromosome 20.";
 Nature 414:865-871(2001).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
 Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
 Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
 Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
 Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
 Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
 Hunkapiller M.W., Myers E.W., Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-373 AND LEU-433.
 TISSUE=Cervix, Placenta, and Uterus;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [5]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21269460; DOI=10.1186/1752-0509-5-17;
 Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
 Bennett K.L., Superti-Furga G., Colinge J.;
 "Initial characterization of the human central proteome.";
 BMC Syst. Biol. 5:17-17(2011).
 [6]
 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
 METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
 [LARGE SCALE ANALYSIS].
 PubMed=22223895; DOI=10.1074/mcp.m111.015131;
 Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
 Giglione C.;
 "Comparative large-scale characterisation of plant vs. mammal proteins
 reveals similar and idiosyncratic N-alpha acetylation features.";
 Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
 [7]
 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
 METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
 [LARGE SCALE ANALYSIS].
 PubMed=22814378; DOI=10.1073/pnas.1210303109;
 Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
 Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
 Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
 "N-terminal acetylome analyses and functional insights of the N-terminal
 acetyltransferase NatB.";
 Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
 [8]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
 Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
 phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [9]
 VARIANTS CDAN2 TRP-14; LYS-109; ALA-348; CYS-497; LEU-603 AND CYS-701, AND
 VARIANT GLN-489.
 PubMed=19621418; DOI=10.1002/humu.21077;
 Bianchi P., Fermo E., Vercellati C., Boschetti C., Barcellini W., Iurlo A.,
 Marcello A.P., Righetti P.G., Zanella A.;
 "Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations
 in the SEC23B gene.";
 Hum. Mutat. 30:1292-1298(2009).
 [10]
 VARIANTS CDAN2 TRP-14; LYS-109 AND TRP-530, VARIANTS HIS-18; GLY-239;
 HIS-313; THR-318; ARG-386; ILE-426; CYS-462; CYS-497 AND VAL-524,
 CHARACTERIZATION OF VARIANTS CDAN2 TRP-14 AND LYS-109, AND CHARACTERIZATION
 OF VARIANT GLY-239.
 PubMed=19561605; DOI=10.1038/ng.405;
 Schwarz K., Iolascon A., Verissimo F., Trede N.S., Horsley W., Chen W.,
 Paw B.H., Hopfner K.-P., Holzmann K., Russo R., Esposito M.R., Spano D.,
 De Falco L., Heinrich K., Joggerst B., Rojewski M.T., Perrotta S.,
 Denecke J., Pannicke U., Delaunay J., Pepperkok R., Heimpel H.;
 "Mutations affecting the secretory COPII coat component SEC23B cause
 congenital dyserythropoietic anemia type II.";
 Nat. Genet. 41:936-940(2009).
 [11]
 VARIANTS CWS7 LEU-164 AND GLY-594, CHARACTERIZATION OF VARIANT CWS7
 GLY-594, INTERACTION WITH SAR1A, AND SUBCELLULAR LOCATION.
 PubMed=26522472; DOI=10.1016/j.ajhg.2015.10.001;
 Yehia L., Niazi F., Ni Y., Ngeow J., Sankunny M., Liu Z., Wei W.,
 Mester J.L., Keri R.A., Zhang B., Eng C.;
 "Germline heterozygous variants in SEC23B are associated with Cowden
 syndrome and enriched in apparently sporadic thyroid cancer.";
 Am. J. Hum. Genet. 97:661-676(2015).
 -!- FUNCTION: Component of the coat protein complex II (COPII) which
     promotes the formation of transport vesicles from the endoplasmic
     reticulum (ER). The coat has two main functions, the physical
     deformation of the endoplasmic reticulum membrane into vesicles and the
     selection of cargo molecules for their transport to the Golgi complex.
     {ECO:0000250|UniProtKB:Q15436}.
 -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
     complex, the Sec13/31 complex and Sar1 (By similarity). Interacts with
     SAR1A (PubMed:26522472). {ECO:0000250|UniProtKB:Q15436,
     ECO:0000269|PubMed:26522472}.
 -!- INTERACTION:
     Q15437; Q8N684: CPSF7; NbExp=3; IntAct=EBI-742673, EBI-746909;
     Q15437; Q86UW9: DTX2; NbExp=6; IntAct=EBI-742673, EBI-740376;
     Q15437; Q969F0: FATE1; NbExp=3; IntAct=EBI-742673, EBI-743099;
     Q15437; O43365: HOXA3; NbExp=4; IntAct=EBI-742673, EBI-8643838;
     Q15437; P42858: HTT; NbExp=3; IntAct=EBI-742673, EBI-466029;
     Q15437; Q96M27: PRRC1; NbExp=3; IntAct=EBI-742673, EBI-2560879;
     Q15437; Q13671: RIN1; NbExp=3; IntAct=EBI-742673, EBI-366017;
     Q15437; Q15436: SEC23A; NbExp=3; IntAct=EBI-742673, EBI-81088;
     Q15437; O94855: SEC24D; NbExp=6; IntAct=EBI-742673, EBI-748817;
     Q15437; O94855-2: SEC24D; NbExp=3; IntAct=EBI-742673, EBI-12081096;
     Q15437; P09234: SNRPC; NbExp=3; IntAct=EBI-742673, EBI-766589;
     Q15437; Q8N205: SYNE4; NbExp=3; IntAct=EBI-742673, EBI-7131783;
 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
     membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein
     {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
     {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane
     {ECO:0000269|PubMed:26522472}; Peripheral membrane protein
     {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
     {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol
     {ECO:0000250|UniProtKB:Q15436}.
 -!- TISSUE SPECIFICITY: Ubiquitously expressed.
     {ECO:0000269|PubMed:8898360}.
 -!- DISEASE: Cowden syndrome 7 (CWS7) [MIM:616858]: A form of Cowden
     syndrome, a hamartomatous polyposis syndrome with age-related
     penetrance. Cowden syndrome is characterized by hamartomatous lesions
     affecting derivatives of ectodermal, mesodermal and endodermal layers,
     macrocephaly, facial trichilemmomas (benign tumors of the hair follicle
     infundibulum), acral keratoses, papillomatous papules, and elevated
     risk for development of several types of malignancy, particularly
     breast carcinoma in women and thyroid carcinoma in both men and women.
     Colon cancer and renal cell carcinoma have also been reported.
     Hamartomas can be found in virtually every organ, but most commonly in
     the skin, gastrointestinal tract, breast and thyroid. CWS7 inheritance
     is autosomal dominant. {ECO:0000269|PubMed:26522472}. Note=The disease
     is caused by variants affecting the gene represented in this entry.
 -!- DISEASE: Anemia, congenital dyserythropoietic, 2 (CDAN2) [MIM:224100]:
     An autosomal recessive blood disorder characterized by morphological
     abnormalities of erythroblasts, ineffective erythropoiesis, normocytic
     anemia, iron overload, jaundice, and variable splenomegaly.
     Ultrastructural features include bi- or multinucleated erythroblasts in
     bone marrow, karyorrhexis, and the presence of Gaucher-like bone marrow
     histiocytes. The main biochemical feature of the disease is defective
     glycosylation of some red blood cells membrane proteins.
     {ECO:0000269|PubMed:19561605, ECO:0000269|PubMed:19621418}. Note=The
     disease is caused by variants affecting the gene represented in this
     entry.
 -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
     {ECO:0000305}.
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 EMBL; X97065; CAA65775.1; -; mRNA.
 EMBL; AL121893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL121900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471133; EAX10231.1; -; Genomic_DNA.
 EMBL; CH471133; EAX10232.1; -; Genomic_DNA.
 EMBL; CH471133; EAX10233.1; -; Genomic_DNA.
 EMBL; CH471133; EAX10234.1; -; Genomic_DNA.
 EMBL; CH471133; EAX10235.1; -; Genomic_DNA.
 EMBL; BC005032; AAH05032.1; -; mRNA.
 EMBL; BC005404; AAH05404.1; -; mRNA.
 EMBL; BC095404; AAH95404.1; -; mRNA.
 CCDS; CCDS13137.1; -.
 RefSeq; NP_001166216.1; NM_001172745.1.
 RefSeq; NP_006354.2; NM_006363.4.
 RefSeq; NP_116780.1; NM_032985.4.
 RefSeq; NP_116781.1; NM_032986.3.
 RefSeq; XP_016883082.1; XM_017027593.1.
 SMR; Q15437; -.
 BioGRID; 115746; 150.
 IntAct; Q15437; 42.
 MINT; Q15437; -.
 STRING; 9606.ENSP00000338844; -.
 iPTMnet; Q15437; -.
 MetOSite; Q15437; -.
 PhosphoSitePlus; Q15437; -.
 BioMuta; SEC23B; -.
 DMDM; 20141794; -.
 EPD; Q15437; -.
 jPOST; Q15437; -.
 MassIVE; Q15437; -.
 MaxQB; Q15437; -.
 PaxDb; Q15437; -.
 PeptideAtlas; Q15437; -.
 PRIDE; Q15437; -.
 ProteomicsDB; 60596; -.
 Antibodypedia; 1407; 181 antibodies.
 DNASU; 10483; -.
 Ensembl; ENST00000262544; ENSP00000262544; ENSG00000101310.
 Ensembl; ENST00000336714; ENSP00000338844; ENSG00000101310.
 Ensembl; ENST00000377465; ENSP00000366685; ENSG00000101310.
 Ensembl; ENST00000650089; ENSP00000497473; ENSG00000101310.
 GeneID; 10483; -.
 KEGG; hsa:10483; -.
 UCSC; uc002wqz.3; human.
 CTD; 10483; -.
 DisGeNET; 10483; -.
 GeneCards; SEC23B; -.
 HGNC; HGNC:10702; SEC23B.
 HPA; ENSG00000101310; Low tissue specificity.
 MalaCards; SEC23B; -.
 MIM; 224100; phenotype.
 MIM; 610512; gene.
 MIM; 616858; phenotype.
 neXtProt; NX_Q15437; -.
 OpenTargets; ENSG00000101310; -.
 Orphanet; 98873; Congenital dyserythropoietic anemia type II.
 Orphanet; 201; Cowden syndrome.
 PharmGKB; PA35625; -.
 VEuPathDB; HostDB:ENSG00000101310.14; -.
 eggNOG; KOG1986; Eukaryota.
 GeneTree; ENSGT00390000006916; -.
 HOGENOM; CLU_008658_3_0_1; -.
 InParanoid; Q15437; -.
 OMA; PWNIIPV; -.
 OrthoDB; 270617at2759; -.
 PhylomeDB; Q15437; -.
 TreeFam; TF300693; -.
 PathwayCommons; Q15437; -.
 BioGRID-ORCS; 10483; 35 hits in 995 CRISPR screens.
 ChiTaRS; SEC23B; human.
 GeneWiki; SEC23B; -.
 GenomeRNAi; 10483; -.
 Pharos; Q15437; Tbio.
 PRO; PR:Q15437; -.
 Proteomes; UP000005640; Chromosome 20.
 RNAct; Q15437; protein.
 Bgee; ENSG00000101310; Expressed in endothelial cell and 236 other tissues.
 ExpressionAtlas; Q15437; baseline and differential.
 Genevisible; Q15437; HS.
 GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
 GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO; GO:0012505; C:endomembrane system; IDA:MGI.
 GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
 GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
 GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
 GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
 CDD; cd11287; Sec23_C; 1.
 Gene3D; 3.40.20.10; -; 1.
 Gene3D; 3.40.50.410; -; 1.
 InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
 InterPro; IPR007123; Gelsolin-like_dom.
 InterPro; IPR036180; Gelsolin-like_dom_sf.
 InterPro; IPR037364; Sec23.
 InterPro; IPR006900; Sec23/24_helical_dom.
 InterPro; IPR036175; Sec23/24_helical_dom_sf.
 InterPro; IPR006896; Sec23/24_trunk_dom.
 InterPro; IPR012990; Sec23_24_beta_S.
 InterPro; IPR037550; Sec23_C.
 InterPro; IPR036465; vWFA_dom_sf.
 InterPro; IPR006895; Znf_Sec23_Sec24.
 InterPro; IPR036174; Znf_Sec23_Sec24_sf.
 PANTHER; PTHR11141; PTHR11141; 1.
 Pfam; PF00626; Gelsolin; 1.
 Pfam; PF08033; Sec23_BS; 1.
 Pfam; PF04815; Sec23_helical; 1.
 Pfam; PF04811; Sec23_trunk; 1.
 Pfam; PF04810; zf-Sec23_Sec24; 1.
 SUPFAM; SSF53300; SSF53300; 1.
 SUPFAM; SSF81811; SSF81811; 1.
 SUPFAM; SSF82754; SSF82754; 1.
 SUPFAM; SSF82919; SSF82919; 1.
 1: Evidence at protein level;
 Acetylation; Congenital dyserythropoietic anemia; Cytoplasm;
 Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum;
 ER-Golgi transport; Hereditary hemolytic anemia; Membrane; Metal-binding;
 Protein transport; Reference proteome; Transport; Zinc.
 INIT_MET        1
                 /note="Removed"
                 /evidence="ECO:0007744|PubMed:22223895,
                 ECO:0007744|PubMed:22814378"
 CHAIN           2..767
                 /note="Protein transport protein Sec23B"
                 /id="PRO_0000205148"
 REPEAT          634..720
                 /note="Gelsolin-like"
                 /evidence="ECO:0000255"
 METAL           61
                 /note="Zinc"
                 /evidence="ECO:0000250|UniProtKB:Q15436"
 METAL           66
                 /note="Zinc"
                 /evidence="ECO:0000250|UniProtKB:Q15436"
 METAL           85
                 /note="Zinc"
                 /evidence="ECO:0000250|UniProtKB:Q15436"
 METAL           88
                 /note="Zinc"
                 /evidence="ECO:0000250|UniProtKB:Q15436"
 MOD_RES         2
                 /note="N-acetylalanine"
                 /evidence="ECO:0007744|PubMed:22223895,
                 ECO:0007744|PubMed:22814378"
 MOD_RES         564
                 /note="N6-acetyllysine"
                 /evidence="ECO:0000250|UniProtKB:Q9D662"
 VARIANT         14
                 /note="R -> W (in CDAN2; the mutant protein is unstable
                 with less than 5% of protein detectable compared to wild-
                 type; dbSNP:rs121918222)"
                 /evidence="ECO:0000269|PubMed:19561605,
                 ECO:0000269|PubMed:19621418"
                 /id="VAR_062294"
 VARIANT         18
                 /note="R -> H (in dbSNP:rs905074313)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062295"
 VARIANT         109
                 /note="E -> K (in CDAN2; the mutant protein is unstable
                 with less than 5% of protein detectable compared to wild-
                 type; dbSNP:rs121918221)"
                 /evidence="ECO:0000269|PubMed:19561605,
                 ECO:0000269|PubMed:19621418"
                 /id="VAR_062296"
 VARIANT         164
                 /note="V -> L (in CWS7; unknown pathological significance;
                 dbSNP:rs36023150)"
                 /evidence="ECO:0000269|PubMed:26522472"
                 /id="VAR_076424"
 VARIANT         239
                 /note="D -> G (the mutant protein is expressed as the wild-
                 type; dbSNP:rs761034212)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062297"
 VARIANT         313
                 /note="R -> H (in dbSNP:rs750888081)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062298"
 VARIANT         318
                 /note="I -> T (in dbSNP:rs953079477)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062299"
 VARIANT         348
                 /note="D -> A (in CDAN2)"
                 /evidence="ECO:0000269|PubMed:19621418"
                 /id="VAR_062300"
 VARIANT         373
                 /note="M -> V (in dbSNP:rs17849992)"
                 /evidence="ECO:0000269|PubMed:15489334"
                 /id="VAR_062301"
 VARIANT         386
                 /note="Q -> R"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062302"
 VARIANT         426
                 /note="V -> I (in dbSNP:rs41309927)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062303"
 VARIANT         433
                 /note="P -> L (in dbSNP:rs17807673)"
                 /evidence="ECO:0000269|PubMed:15489334"
                 /id="VAR_034482"
 VARIANT         462
                 /note="Y -> C (in dbSNP:rs780978419)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062304"
 VARIANT         489
                 /note="H -> Q (in dbSNP:rs2273526)"
                 /evidence="ECO:0000269|PubMed:19621418,
                 ECO:0000269|PubMed:8898360"
                 /id="VAR_020318"
 VARIANT         497
                 /note="R -> C (in CDAN2; unknown pathological significance;
                 dbSNP:rs727504145)"
                 /evidence="ECO:0000269|PubMed:19561605,
                 ECO:0000269|PubMed:19621418"
                 /id="VAR_062305"
 VARIANT         524
                 /note="A -> V (in dbSNP:rs398124225)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062306"
 VARIANT         530
                 /note="R -> W (in CDAN2; dbSNP:rs121918223)"
                 /evidence="ECO:0000269|PubMed:19561605"
                 /id="VAR_062307"
 VARIANT         594
                 /note="V -> G (in CWS7; aberrant aggregation; causes
                 mislocalization of the protein in the cytoplasm; reduces
                 interaction with SAR1A; confers endoplasmic reticulum (ER)
                 stress-mediated cell growth advantage; dbSNP:rs752366963)"
                 /evidence="ECO:0000269|PubMed:26522472"
                 /id="VAR_076425"
 VARIANT         603
                 /note="S -> L (in CDAN2)"
                 /evidence="ECO:0000269|PubMed:19621418"
                 /id="VAR_062308"
 VARIANT         701
                 /note="R -> C (in CDAN2; dbSNP:rs201270568)"
                 /evidence="ECO:0000269|PubMed:19621418"
                 /id="VAR_062309"
 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

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