ID SC23A_HUMAN Reviewed; 765 AA. AC Q15436; B2R5P4; B3KXI2; Q8NE16; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 2. DT 02-SEP-2026, entry version 221. DE RecName: Full=Protein transport protein Sec23A {ECO:0000305}; DE Short=hSec23A {ECO:0000303|PubMed:8898360}; DE AltName: Full=SEC23-related protein A; GN Name=SEC23A {ECO:0000312|HGNC:HGNC:10701}; 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), VARIANT VAL-211, FUNCTION, RP SUBCELLULAR LOCATION, TOPOLOGY, 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 MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP VAL-211. RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-211. RC TISSUE=Testis; 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 INTERACTION WITH SEC16A. RC TISSUE=Liver; RX PubMed=17192411; DOI=10.1091/mbc.e06-08-0707; RA Bhattacharyya D., Glick B.S.; RT "Two mammalian Sec16 homologues have nonredundant functions in endoplasmic RT reticulum (ER) export and transitional ER organization."; RL Mol. Biol. Cell 18:839-849(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, AND IDENTIFICATION BY RP 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 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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 [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] RP INTERACTION WITH MIA3, AND SUBCELLULAR LOCATION. RX PubMed=28442536; DOI=10.1083/jcb.201703084; RA Maeda M., Katada T., Saito K.; RT "TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient RT secretion."; RL J. Cell Biol. 216:1731-1743(2017). RN [13] RP INTERACTION WITH TMEM39A AND SACM1L. RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035; RA Miao G., Zhang Y., Chen D., Zhang H.; RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1."; RL Mol. Cell 0:0-0(2019). RN [14] RP INTERACTION WITH FAM20C. RX PubMed=34349020; DOI=10.1073/pnas.2100133118; RA Chen X., Zhang J., Liu P., Wei Y., Wang X., Xiao J., Wang C.C., Wang L.; RT "Proteolytic processing of secretory pathway kinase Fam20C by site-1 RT protease promotes biomineralization."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [15] {ECO:0007744|PDB:2YRC, ECO:0007744|PDB:2YRD} RP STRUCTURE BY NMR OF 57-108 IN COMPLEX WITH ZINC. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the ZF-SEC23_SEC24 from human SEC23A."; RL Submitted (OCT-2007) to the PDB data bank. RN [16] {ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2NUT} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SEC22B; SEC24A AND RP ZINC, FUNCTION, SUBUNIT, AND INTERACTION WITH SEC22B. 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 [17] {ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, ECO:0007744|PDB:3EGD, ECO:0007744|PDB:3EGX} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-764 IN COMPLEX WITH CARGO RP PEPTIDES; SEC22B; SEC24A; SEC24D AND ZINC, 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 [18] {ECO:0007744|PDB:5KYN, ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYW, ECO:0007744|PDB:5KYX, ECO:0007744|PDB:5KYY} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH MIA3 PEPTIDE; SEC24D RP AND ZINC, FUNCTION, INTERACTION WITH MIA2; MIA3 AND SEC31A, MUTAGENESIS OF RP PHE-628; TYR-672; TYR-678 AND PHE-681, AND DOMAIN. RX PubMed=27551091; DOI=10.1073/pnas.1605916113; RA Ma W., Goldberg J.; RT "TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large RT COPII coats."; RL Proc. Natl. Acad. Sci. U.S.A. 113:10061-10066(2016). RN [19] RP VARIANT CLSD LEU-382, CHARACTERIZATION OF VARIANT CLSD LEU-382, AND RP FUNCTION. RX PubMed=16980979; DOI=10.1038/ng1876; RA Boyadjiev S.A., Fromme J.C., Ben J., Chong S.S., Nauta C., Hur D.J., RA Zhang G., Hamamoto S., Schekman R., Ravazzola M., Orci L., Eyaid W.; RT "Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading RT to abnormal endoplasmic-reticulum-to-Golgi trafficking."; RL Nat. Genet. 38:1192-1197(2006). 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 Required for the translocation of insulin-induced glucose transporter CC SLC2A4/GLUT4 to the cell membrane (By similarity). CC {ECO:0000250|UniProtKB:Q01405, ECO:0000269|PubMed:16980979, CC ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296, CC ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:8898360}. CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24 CC complex, the Sec13/31 complex and Sar1 (PubMed:17499046). Interacts CC with SEC23IP. Interacts with HTR4 (By similarity). Interacts with CC SEC16A (PubMed:17192411). Interacts with SLC6A4 (By similarity). CC Interacts (as part of the Sec23/24 complex) with SEC22B; recruits CC SEC22B into COPII-coated vesicles and allows the transport of this CC cargo from the endoplasmic reticulum to the Golgi (PubMed:17499046). CC Interacts (via Gelsolin-like repeat) with MIA2 and MIA3; specifically CC involved in the transport of large cargos like the collagen COL7A1 CC (PubMed:27551091, PubMed:28442536). Interacts with DDHD1 (By CC similarity). Interacts with TMEM39A (PubMed:31806350). Interacts with CC SACM1L; this interaction is reduced in the absence of TMEM39A CC (PubMed:31806350). Interacts with kinase FAM20C; transport of FAM20C CC from the endoplasmic reticulum to the Golgi is likely to be mediated by CC COPII vesicles (PubMed:34349020). {ECO:0000250|UniProtKB:Q01405, CC ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17499046, CC ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:28442536, CC ECO:0000269|PubMed:31806350, ECO:0000269|PubMed:34349020}. CC -!- INTERACTION: CC Q15436; Q12983: BNIP3; NbExp=3; IntAct=EBI-81088, EBI-749464; CC Q15436; A2RRN7: CADPS; NbExp=3; IntAct=EBI-81088, EBI-10179719; CC Q15436; Q00536: CDK16; NbExp=3; IntAct=EBI-81088, EBI-726261; CC Q15436; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-81088, EBI-11977093; CC Q15436; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-81088, EBI-25840379; CC Q15436; P50570: DNM2; NbExp=3; IntAct=EBI-81088, EBI-346547; CC Q15436; Q86UW9: DTX2; NbExp=3; IntAct=EBI-81088, EBI-740376; CC Q15436; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-81088, EBI-781551; CC Q15436; O75477: ERLIN1; NbExp=3; IntAct=EBI-81088, EBI-359299; CC Q15436; P48023: FASLG; NbExp=3; IntAct=EBI-81088, EBI-495538; CC Q15436; Q969F0: FATE1; NbExp=3; IntAct=EBI-81088, EBI-743099; CC Q15436; P48165: GJA8; NbExp=3; IntAct=EBI-81088, EBI-17458373; CC Q15436; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-81088, EBI-11956541; CC Q15436; Q5JRA6: MIA3; NbExp=3; IntAct=EBI-81088, EBI-2291868; CC Q15436; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-81088, EBI-11977115; CC Q15436; O75928-2: PIAS2; NbExp=3; IntAct=EBI-81088, EBI-348567; CC Q15436; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-81088, EBI-2466594; CC Q15436; Q15437: SEC23B; NbExp=6; IntAct=EBI-81088, EBI-742673; CC Q15436; Q9Y6Y8: SEC23IP; NbExp=5; IntAct=EBI-81088, EBI-1767971; CC Q15436; O95487: SEC24B; NbExp=4; IntAct=EBI-81088, EBI-81101; CC Q15436; P53992: SEC24C; NbExp=8; IntAct=EBI-81088, EBI-81134; CC Q15436; O94855: SEC24D; NbExp=5; IntAct=EBI-81088, EBI-748817; CC Q15436; O94855-2: SEC24D; NbExp=3; IntAct=EBI-81088, EBI-12081096; CC Q15436; Q15637-4: SF1; NbExp=3; IntAct=EBI-81088, EBI-12223157; CC Q15436; P30825: SLC7A1; NbExp=3; IntAct=EBI-81088, EBI-4289564; CC Q15436; Q9P2R7: SUCLA2; NbExp=3; IntAct=EBI-81088, EBI-2269898; CC Q15436; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-81088, EBI-3923061; CC Q15436; O43557: TNFSF14; NbExp=3; IntAct=EBI-81088, EBI-524131; CC Q15436; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-81088, EBI-714455; CC Q15436; P0DTC2: S; Xeno; NbExp=20; IntAct=EBI-81088, EBI-25474821; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle CC membrane {ECO:0000305|PubMed:8898360}; Peripheral membrane protein CC {ECO:0000269|PubMed:8898360}; Cytoplasmic side CC {ECO:0000269|PubMed:8898360}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:8898360}; Peripheral membrane protein CC {ECO:0000269|PubMed:8898360}; Cytoplasmic side CC {ECO:0000269|PubMed:8898360}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:8898360}. Note=Enriched at endoplasmic reticulum CC exit sites, also known as transitional endoplasmic reticulum (tER). CC {ECO:0000269|PubMed:28442536, ECO:0000269|PubMed:8898360}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15436-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15436-2; Sequence=VSP_056230; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:8898360}. CC -!- DOMAIN: The Gelsolin-like repeat mediates interaction with proteins CC containing PPP motifs that include MIA2, MIA3 but also SEC31A. These CC interactions are probably competitive. {ECO:0000269|PubMed:27551091}. CC -!- DISEASE: Craniolenticulosutural dysplasia (CLSD) [MIM:607812]: CC Autosomal recessive syndrome characterized by late-closing fontanels, CC sutural cataracts, facial dysmorphisms and skeletal defects. CC {ECO:0000269|PubMed:16980979}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X97064; CAA65774.1; -; mRNA. DR EMBL; AK127355; BAG54494.1; -; mRNA. DR EMBL; AK312259; BAG35191.1; -; mRNA. DR EMBL; AL109628; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC036649; AAH36649.1; -; mRNA. DR CCDS; CCDS9668.1; -. [Q15436-1] DR PIR; T09574; T09574. DR RefSeq; NP_006355.2; NM_006364.4. [Q15436-1] DR PDB; 2NUP; X-ray; 2.80 A; A=1-765. DR PDB; 2NUT; X-ray; 2.30 A; A=1-765. DR PDB; 2YRC; NMR; -; A=57-108. DR PDB; 2YRD; NMR; -; A=57-108. DR PDB; 3EFO; X-ray; 2.70 A; A=1-765. DR PDB; 3EG9; X-ray; 3.00 A; A=1-764. DR PDB; 3EGD; X-ray; 2.70 A; A=1-764. DR PDB; 3EGX; X-ray; 3.30 A; A=1-764. DR PDB; 5KYN; X-ray; 2.55 A; A/B=1-765. DR PDB; 5KYU; X-ray; 3.51 A; A=1-765. DR PDB; 5KYW; X-ray; 3.20 A; A=1-765. DR PDB; 5KYX; X-ray; 3.52 A; A=1-765. DR PDB; 5KYY; X-ray; 3.40 A; A=1-765. DR PDB; 5VNE; X-ray; 2.70 A; A=1-764. DR PDB; 5VNF; X-ray; 2.41 A; A=1-764. DR PDB; 5VNG; X-ray; 2.60 A; A=1-764. DR PDB; 5VNH; X-ray; 2.60 A; A=1-764. DR PDB; 5VNI; X-ray; 2.79 A; A=1-764. DR PDB; 5VNJ; X-ray; 2.81 A; A=1-764. DR PDB; 5VNK; X-ray; 2.55 A; A=1-764. DR PDB; 5VNL; X-ray; 2.39 A; A=1-764. DR PDB; 5VNM; X-ray; 2.77 A; A=1-764. DR PDB; 5VNN; X-ray; 2.50 A; A=1-764. DR PDB; 5VNO; X-ray; 2.90 A; A=1-764. DR PDB; 8HR0; X-ray; 3.34 A; A=1-765. DR PDB; 9UVD; X-ray; 2.98 A; A=1-765. DR PDB; 9UVE; X-ray; 2.60 A; A=1-765. DR PDB; 9UVF; X-ray; 3.15 A; A=1-765. DR PDB; 9UVG; X-ray; 2.54 A; A=1-765. DR AlphaFoldDB; Q15436; -. DR SMR; Q15436; -. DR BioGRID; 115747; 262. DR CORUM; Q15436; -. DR FunCoup; Q15436; 2611. DR IntAct; Q15436; 124. DR MINT; Q15436; -. DR NDEx; IQUERY-CP-SEC23A; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000306881; -. DR BindingDB; Q15436; -. DR ChEMBL; CHEMBL4295827; -. DR GlyCosmos; Q15436; 12 sites, 1 glycan. DR GlyGen; Q15436; 34 sites, 1 O-linked glycan (34 sites). DR iPTMnet; Q15436; -. DR MetOSite; Q15436; -. DR PhosphoSitePlus; Q15436; -. DR SwissPalm; Q15436; -. DR BioMuta; SEC23A; -. DR DMDM; 143811354; -. DR jPOST; Q15436; -. DR MassIVE; Q15436; -. DR PaxDb; 9606-ENSP00000306881; -. DR PeptideAtlas; Q15436; -. DR ProteomicsDB; 3813; -. DR ProteomicsDB; 60595; -. [Q15436-1] DR Pumba; Q15436; -. DR Antibodypedia; 23326; 177 antibodies from 36 providers. DR DNASU; 10484; -. DR Ensembl; ENST00000307712.11; ENSP00000306881.6; ENSG00000100934.16. [Q15436-1] DR Ensembl; ENST00000537403.5; ENSP00000444193.1; ENSG00000100934.16. [Q15436-2] DR Ensembl; ENST00000857743.1; ENSP00000527802.1; ENSG00000100934.16. [Q15436-1] DR Ensembl; ENST00000919376.1; ENSP00000589435.1; ENSG00000100934.16. [Q15436-1] DR Ensembl; ENST00000945648.1; ENSP00000615707.1; ENSG00000100934.16. [Q15436-1] DR GeneID; 10484; -. DR KEGG; hsa:10484; -. DR MANE-Select; ENST00000307712.11; ENSP00000306881.6; NM_006364.4; NP_006355.2. DR UCSC; uc001wup.2; human. [Q15436-1] DR AGR; HGNC:10701; -. DR ClinPGx; PA35624; -. DR CTD; 10484; -. DR DisGeNET; 10484; -. DR GeneCards; SEC23A; -. DR HGNC; HGNC:10701; SEC23A. DR HPA; ENSG00000100934; Low tissue specificity. DR MalaCards; SEC23A; -. DR MIM; 607812; phenotype. DR MIM; 610511; gene. DR OpenTargets; ENSG00000100934; -. DR Orphanet; 50814; Craniolenticulosutural dysplasia. DR VEuPathDB; HostDB:ENSG00000100934; -. DR eggNOG; KOG1986; Eukaryota. DR GeneTree; ENSGT00390000006916; -. DR HOGENOM; CLU_008658_4_0_1; -. DR InParanoid; Q15436; -. DR OMA; LFHGERE; -. DR OrthoDB; 10256289at2759; -. DR PAN-GO; Q15436; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q15436; -. DR PathwayCommons; Q15436; -. 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; Q15436; -. DR SIGNOR; Q15436; -. DR Agora; ENSG00000100934; -. DR BioGRID-ORCS; 10484; 21 hits in 1151 CRISPR screens. DR CD-CODE; 1EF72FBA; ERES. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; SEC23A; human. DR EvolutionaryTrace; Q15436; -. DR GeneWiki; SEC23A; -. DR GenomeRNAi; 10484; -. DR Pharos; Q15436; Tbio. DR PRO; PR:Q15436; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q15436; protein. DR Bgee; ENSG00000100934; Expressed in jejunal mucosa and 214 other cell types or tissues. DR ExpressionAtlas; Q15436; baseline and differential. DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; EXP:UniProtKB. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IGI:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl. 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; IDA:UniProtKB. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB. DR GO; GO:0032456; P:endocytic recycling; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR CDD; cd01478; Sec23-like; 1. DR CDD; cd11287; Sec23_C; 1. DR FunFam; 1.20.120.730:FF:000003; Protein transport protein SEC23; 1. DR FunFam; 2.30.30.380:FF:000001; Protein transport protein SEC23; 1. DR FunFam; 2.60.40.1670:FF:000006; Protein transport protein SEC23; 1. DR FunFam; 3.40.20.10:FF:000003; Protein transport protein SEC23; 1. DR FunFam; 3.40.50.410:FF:000011; Protein transport protein SEC23; 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; IPR012990; Beta-sandwich_Sec23_24. 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; 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; PROTEIN TRANSPORT PROTEIN SEC23; 1. DR PANTHER; PTHR11141:SF7; PROTEIN TRANSPORT PROTEIN SEC23A; 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. DR PDBsum; 2NUP; -. DR PDBsum; 2NUT; -. DR PDBsum; 2YRC; -. DR PDBsum; 2YRD; -. DR PDBsum; 3EFO; -. DR PDBsum; 3EG9; -. DR PDBsum; 3EGD; -. DR PDBsum; 3EGX; -. DR PDBsum; 5KYN; -. DR PDBsum; 5KYU; -. DR PDBsum; 5KYW; -. DR PDBsum; 5KYX; -. DR PDBsum; 5KYY; -. DR PDBsum; 5VNE; -. DR PDBsum; 5VNF; -. DR PDBsum; 5VNG; -. DR PDBsum; 5VNH; -. DR PDBsum; 5VNI; -. DR PDBsum; 5VNJ; -. DR PDBsum; 5VNK; -. DR PDBsum; 5VNL; -. DR PDBsum; 5VNM; -. DR PDBsum; 5VNN; -. DR PDBsum; 5VNO; -. DR PDBsum; 8HR0; -. DR PDBsum; 9UVD; -. DR PDBsum; 9UVE; -. DR PDBsum; 9UVF; -. DR PDBsum; 9UVG; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum; KW ER-Golgi transport; Membrane; Metal-binding; Phosphoprotein; KW Protein transport; Proteomics identification; Reference proteome; KW Transport; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..765 FT /note="Protein transport protein Sec23A" FT /id="PRO_0000205146" FT REPEAT 632..718 FT /note="Gelsolin-like" FT /evidence="ECO:0000255" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD, FT ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD, FT ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD, FT ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2YRD, FT ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, FT ECO:0007744|PDB:3EGD, ECO:0007744|PDB:5KYN, FT ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 308 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..202 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056230" FT VARIANT 211 FT /note="L -> V (in dbSNP:rs8018720)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8898360" FT /id="VAR_031029" FT VARIANT 382 FT /note="F -> L (in CLSD; loss of COPII vesicle coating; FT results in absence of incorporation of cargo proteins into FT vesicles; dbSNP:rs118204000)" FT /evidence="ECO:0000269|PubMed:16980979" FT /id="VAR_031030" FT MUTAGEN 628 FT /note="F->A: Decreased interaction with MIA3; when FT associated with A-681." FT /evidence="ECO:0000269|PubMed:27551091" FT MUTAGEN 672 FT /note="Y->K: Decreased interaction with MIA3; when FT associated with A-678." FT /evidence="ECO:0000269|PubMed:27551091" FT MUTAGEN 678 FT /note="Y->A: Decreased interaction with MIA3; when FT associated with K-672." FT /evidence="ECO:0000269|PubMed:27551091" FT MUTAGEN 681 FT /note="F->A: Decreased interaction with MIA3; when FT associated with A-628." FT /evidence="ECO:0000269|PubMed:27551091" FT CONFLICT 623 FT /note="L -> M (in Ref. 4; AAH36649)" FT /evidence="ECO:0000305" FT HELIX 4..15 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 16..24 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:5KYN" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:5VNL" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:5VNL" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:5VNL" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:2NUT" FT TURN 78..81 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:5VNL" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 125..129 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 141..155 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 163..179 FT /evidence="ECO:0007829|PDB:2NUT" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:5VNL" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 198..204 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 233..246 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:5VNJ" FT HELIX 264..278 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 285..292 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 313..317 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 324..341 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 344..350 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 362..366 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 371..375 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 380..388 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:8HR0" FT STRAND 401..410 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 414..422 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:3EG9" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:5VNL" FT STRAND 444..451 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 457..463 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:3EG9" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:5KYN" FT STRAND 477..487 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:2NUP" FT STRAND 492..501 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 506..508 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 509..515 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 519..534 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 542..557 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 558..561 FT /evidence="ECO:0007829|PDB:3EGD" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:2NUT" FT TURN 572..576 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 577..586 FT /evidence="ECO:0007829|PDB:2NUT" FT TURN 588..590 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 592..594 FT /evidence="ECO:0007829|PDB:3EFO" FT HELIX 597..607 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 612..619 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 622..626 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 628..631 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:5VNF" FT HELIX 639..641 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 647..651 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 653..660 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 662..670 FT /evidence="ECO:0007829|PDB:2NUT" FT TURN 671..674 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 676..678 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 679..698 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 699..701 FT /evidence="ECO:0007829|PDB:2NUT" FT STRAND 704..709 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 713..715 FT /evidence="ECO:0007829|PDB:5VNL" FT HELIX 716..721 FT /evidence="ECO:0007829|PDB:2NUT" FT HELIX 749..760 FT /evidence="ECO:0007829|PDB:2NUT" SQ SEQUENCE 765 AA; 86161 MW; 128DF9964B253313 CRC64; MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD LPPIQYEPVL CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG ISELNQPAEL LPQFSSIEYV VLRGPQMPLI FLYVVDTCME DEDLQALKES MQMSLSLLPP TALVGLITFG RMVQVHELGC EGISKSYVFR GTKDLSAKQL QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL TDLLGELQRD PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC ALDQTGLLEM KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM GFGGTLEIKT SREIKISGAI GPCVSLNSKG PCVSENEIGT GGTCQWKICG LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ FVTQYQHSSG QRRIRVTTIA RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP DVLRWLDRQL IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM DTFFQILIYH GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF PMPRYIDTEH GGSQARFLLS KVNPSQTHNN MYAWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA //