SC23A_HUMAN
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 03-AUG-2022, entry version 203.
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=3; IntAct=EBI-81088, EBI-742673;
CC Q15436; Q9Y6Y8: SEC23IP; NbExp=3; IntAct=EBI-81088, EBI-1767971;
CC Q15436; P53992: SEC24C; NbExp=5; IntAct=EBI-81088, EBI-81134;
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}.
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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_006364.3. [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 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 AlphaFoldDB; Q15436; -.
DR SMR; Q15436; -.
DR BioGRID; 115747; 181.
DR CORUM; Q15436; -.
DR IntAct; Q15436; 78.
DR MINT; Q15436; -.
DR STRING; 9606.ENSP00000306881; -.
DR ChEMBL; CHEMBL4295827; -.
DR GlyGen; Q15436; 12 sites, 1 O-linked glycan (12 sites).
DR iPTMnet; Q15436; -.
DR MetOSite; Q15436; -.
DR PhosphoSitePlus; Q15436; -.
DR SwissPalm; Q15436; -.
DR BioMuta; SEC23A; -.
DR DMDM; 143811354; -.
DR EPD; Q15436; -.
DR jPOST; Q15436; -.
DR MassIVE; Q15436; -.
DR MaxQB; Q15436; -.
DR PaxDb; Q15436; -.
DR PeptideAtlas; Q15436; -.
DR PRIDE; Q15436; -.
DR ProteomicsDB; 3813; -.
DR ProteomicsDB; 60595; -. [Q15436-1]
DR Antibodypedia; 23326; 166 antibodies from 33 providers.
DR DNASU; 10484; -.
DR Ensembl; ENST00000307712.11; ENSP00000306881.6; ENSG00000100934.15. [Q15436-1]
DR Ensembl; ENST00000537403.5; ENSP00000444193.1; ENSG00000100934.15. [Q15436-2]
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 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 neXtProt; NX_Q15436; -.
DR OpenTargets; ENSG00000100934; -.
DR Orphanet; 50814; Craniolenticulosutural dysplasia.
DR PharmGKB; PA35624; -.
DR VEuPathDB; HostDB:ENSG00000100934; -.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_4_0_1; -.
DR InParanoid; Q15436; -.
DR OMA; SKCVIPV; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; Q15436; -.
DR TreeFam; TF300693; -.
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 BioGRID-ORCS; 10484; 20 hits in 1073 CRISPR screens.
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 212 other tissues.
DR ExpressionAtlas; Q15436; baseline and differential.
DR Genevisible; Q15436; 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; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IGI:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA: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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Cytoplasmic vesicle; Disease variant; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Metal-binding; Phosphoprotein;
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..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 STRAND 49..51
FT /evidence="ECO:0007829|PDB:5KYY"
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 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 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 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 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 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
