SC23A_MOUSE
ID SC23A_MOUSE Reviewed; 765 AA.
AC Q01405; Q8JZL4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein transport protein Sec23A {ECO:0000305};
DE AltName: Full=SEC23-related protein A;
GN Name=Sec23a {ECO:0000312|MGI:MGI:1349635}; Synonyms=Sec23, Sec23r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12193656; DOI=10.1073/pnas.182412799;
RA Espenshade P.J., Li W.-P., Yabe D.;
RT "Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP
RT sorting in ER.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11694-11699(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-631, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=8417978; DOI=10.1016/0014-5793(93)81161-r;
RA Wadhwa R., Kaul S.C., Komatsu Y., Ikawa Y., Sarai A., Sugimoto Y.;
RT "Identification and differential expression of yeast SEC23-related gene
RT (Msec23) in mouse tissues.";
RL FEBS Lett. 315:193-196(1993).
RN [4]
RP INTERACTION WITH SEC23IP.
RX PubMed=10400679; DOI=10.1074/jbc.274.29.20505;
RA Tani K., Mizoguchi T., Iwamatsu A., Hatsuzawa K., Tagaya M.;
RT "p125 is a novel mammalian Sec23p-interacting protein with structural
RT similarity to phospholipid-modifying proteins.";
RL J. Biol. Chem. 274:20505-20512(1999).
RN [5]
RP INTERACTION WITH HTR4.
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [6]
RP INTERACTION WITH SEC16A AND DDHD1.
RX PubMed=17428803; DOI=10.1074/jbc.m611237200;
RA Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N.,
RA Tagaya M., Tani K.;
RT "Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 282:17632-17639(2007).
RN [7]
RP INTERACTION WITH SLC6A4.
RX PubMed=17452640; DOI=10.1073/pnas.0610964104;
RA Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
RA Freissmuth M., Millan M.J., Bockaert J., Marin P.;
RT "Physical interaction between the serotonin transporter and neuronal nitric
RT oxide synthase underlies reciprocal modulation of their activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION.
RX PubMed=27354378; DOI=10.1083/jcb.201509052;
RA Bruno J., Brumfield A., Chaudhary N., Iaea D., McGraw T.E.;
RT "SEC16A is a RAB10 effector required for insulin-stimulated GLUT4
RT trafficking in adipocytes.";
RL J. Cell Biol. 214:61-76(2016).
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 (By similarity). Required for the translocation of insulin-induced
CC glucose transporter SLC2A4/GLUT4 to the cell membrane
CC (PubMed:27354378). {ECO:0000250|UniProtKB:Q15436,
CC ECO:0000269|PubMed:27354378}.
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 SEC23IP (PubMed:10400679). Interacts with HTR4 (PubMed:15466885).
CC Interacts with SEC16A (PubMed:17428803). Interacts with SLC6A4
CC (PubMed:17452640). Interacts (as part of the Sec23/24 complex) with
CC SEC22B; recruits SEC22B into COPII-coated vesicles and allows the
CC transport of this cargo from the endoplasmic reticulum to the Golgi.
CC Interacts (via Gelsolin-like repeat) with MIA2 and MIA3; specifically
CC involved in the transport of large cargos like the collagen COL7A1 (By
CC similarity). Interacts with DDHD1 (PubMed:17428803). Interacts with
CC TMEM39A (By similarity). Interacts with SACM1L; this interaction is
CC reduced in the absence of TMEM39A (By similarity). Interacts with
CC kinase FAM20C; transport of FAM20C from the endoplasmic reticulum to
CC the Golgi is likely to be mediated by COPII vesicles (By similarity).
CC {ECO:0000250|UniProtKB:Q15436, ECO:0000269|PubMed:10400679,
CC ECO:0000269|PubMed:15466885, ECO:0000269|PubMed:17428803,
CC ECO:0000269|PubMed:17452640}.
CC -!- INTERACTION:
CC Q01405; Q9NR31: SAR1A; Xeno; NbExp=2; IntAct=EBI-775901, EBI-3920694;
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:0000250|UniProtKB:Q15436}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15436}. Note=Enriched at endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). {ECO:0000250|UniProtKB:Q15436}.
CC -!- TISSUE SPECIFICITY: High levels in brain and fibroblasts.
CC {ECO:0000269|PubMed:8417978}.
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:0000250|UniProtKB:Q15436}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02209.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY082671; AAL92480.1; -; mRNA.
DR EMBL; BC034610; AAH34610.1; -; mRNA.
DR EMBL; D12713; BAA02209.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS25931.1; -.
DR PIR; S28142; I60247.
DR RefSeq; NP_033173.2; NM_009147.2.
DR RefSeq; XP_006515691.1; XM_006515628.3.
DR AlphaFoldDB; Q01405; -.
DR SMR; Q01405; -.
DR BioGRID; 203150; 29.
DR DIP; DIP-32032N; -.
DR IntAct; Q01405; 8.
DR MINT; Q01405; -.
DR STRING; 10090.ENSMUSP00000021375; -.
DR iPTMnet; Q01405; -.
DR PhosphoSitePlus; Q01405; -.
DR SwissPalm; Q01405; -.
DR EPD; Q01405; -.
DR jPOST; Q01405; -.
DR MaxQB; Q01405; -.
DR PaxDb; Q01405; -.
DR PeptideAtlas; Q01405; -.
DR PRIDE; Q01405; -.
DR ProteomicsDB; 256734; -.
DR Antibodypedia; 23326; 166 antibodies from 33 providers.
DR DNASU; 20334; -.
DR Ensembl; ENSMUST00000021375; ENSMUSP00000021375; ENSMUSG00000020986.
DR GeneID; 20334; -.
DR KEGG; mmu:20334; -.
DR UCSC; uc007npw.1; mouse.
DR CTD; 10484; -.
DR MGI; MGI:1349635; Sec23a.
DR VEuPathDB; HostDB:ENSMUSG00000020986; -.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR InParanoid; Q01405; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR PhylomeDB; Q01405; -.
DR TreeFam; TF300693; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 20334; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sec23a; mouse.
DR PRO; PR:Q01405; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q01405; protein.
DR Bgee; ENSMUSG00000020986; Expressed in vault of skull and 268 other tissues.
DR ExpressionAtlas; Q01405; baseline and differential.
DR Genevisible; Q01405; MM.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
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; Cytoplasm; Cytoplasmic vesicle; 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:0000250|UniProtKB:Q15436"
FT CHAIN 2..765
FT /note="Protein transport protein Sec23A"
FT /id="PRO_0000205147"
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: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-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT CONFLICT 81..83
FT /note="KLW -> TR (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..92
FT /note="RN -> D (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> S (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="A -> R (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..117
FT /note="SSI -> QS (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="L -> F (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..157
FT /note="MSLSL -> TTFS (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="M -> I (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="RG -> S (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> P (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="P -> S (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="I -> M (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="A -> R (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="A -> P (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="P -> R (in Ref. 3; BAA02209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 86162 MW; C0FD4C2C1578B6A5 CRC64;
MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD LPPIQYEPVL
CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPTYAG ISELNQPAEL LPQFSSIEYV
VLRGPQMPLI FLYVVDTCIE DEDLQALKES MQMSLSLLPP TALVGLITFG RMVQVHELGC
EGISKSYVFR GTKDLSAKQL QEMLGLSKVP VTQATRGPQV QQPPPSNRFL QPVQKIDMNL
TDLLGELQRD PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM
VVGDELKTPI RSWHDIEKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC ALDQTGLLEM
KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDIHGQFKM GFGGTLEIKT SREIKISGAI
GPCVSLNSKG PCVSENEIGT GGTCQWKICG LSPTTTLAIY FEVVNQHNAP IPQGGRGAVQ
FVTQYQHSSG QRRIRVTTIA RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP
DVLRWLDRQL IRLCQKFGEY HKDDPNSFRF SETFSLYPQF MFHLRRSPFL QVFNNSPDES
SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM DTFFQILIYH
GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF PMPRYIDTEH GGSQARFLLS
KVNPSQTHNN MYAWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA
