SC24A_MOUSE
ID SC24A_MOUSE Reviewed; 1090 AA.
AC Q3U2P1; A2AA70; A2AA73; A4FUV4; Q3TQ05; Q3TRG7; Q8BIS0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein transport protein Sec24A {ECO:0000305};
DE AltName: Full=SEC24-related protein A;
GN Name=Sec24a {ECO:0000312|MGI:MGI:1924621};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-1090.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
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).
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 Plays a central role in cargo selection within the COPII complex and
CC together with SEC24B may have a different specificity compared to
CC SEC24C and SEC24D. May package preferentially cargos with cytoplasmic
CC DxE or LxxLE motifs and may also recognize conformational epitopes.
CC {ECO:0000250|UniProtKB:O95486}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1. Interacts with TMED2. Interacts
CC (as part of the Sec23/24 complex) with SEC22B; recruits SEC22B into
CC COPII-coated vesicles for its transport from the endoplasmic reticulum
CC to the Golgi (By similarity). Interacts with STING1; promoting STING1
CC translocation to COPII vesicles in a STEEP1-dependent manner (By
CC similarity). Interacts with TMEM39A (By similarity). Interacts with
CC SACM1L; this interaction is reduced in the absence of TMEM39A (By
CC similarity). Interacts with kinase FAM20C; transport of FAM20C from the
CC endoplasmic reticulum to the Golgi is likely to be mediated by COPII
CC vesicles (By similarity). {ECO:0000250|UniProtKB:O95486}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95486}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95486}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95486}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95486}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95486}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O95486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U2P1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U2P1-2; Sequence=VSP_016990, VSP_016991;
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26319.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK029139; BAC26319.1; ALT_SEQ; mRNA.
DR EMBL; AK155182; BAE33099.1; -; mRNA.
DR EMBL; AK162795; BAE37062.1; -; mRNA.
DR EMBL; AK163998; BAE37580.1; -; mRNA.
DR EMBL; AL645602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117905; AAI17906.1; -; mRNA.
DR CCDS; CCDS24660.2; -. [Q3U2P1-1]
DR RefSeq; NP_001277714.1; NM_001290785.1.
DR RefSeq; NP_780464.2; NM_175255.3. [Q3U2P1-1]
DR AlphaFoldDB; Q3U2P1; -.
DR SMR; Q3U2P1; -.
DR BioGRID; 218649; 9.
DR STRING; 10090.ENSMUSP00000104725; -.
DR iPTMnet; Q3U2P1; -.
DR PhosphoSitePlus; Q3U2P1; -.
DR EPD; Q3U2P1; -.
DR jPOST; Q3U2P1; -.
DR MaxQB; Q3U2P1; -.
DR PaxDb; Q3U2P1; -.
DR PeptideAtlas; Q3U2P1; -.
DR PRIDE; Q3U2P1; -.
DR ProteomicsDB; 255343; -. [Q3U2P1-1]
DR ProteomicsDB; 255344; -. [Q3U2P1-2]
DR Antibodypedia; 45232; 111 antibodies from 24 providers.
DR DNASU; 77371; -.
DR Ensembl; ENSMUST00000064297; ENSMUSP00000068065; ENSMUSG00000036391. [Q3U2P1-2]
DR Ensembl; ENSMUST00000109097; ENSMUSP00000104725; ENSMUSG00000036391. [Q3U2P1-1]
DR GeneID; 77371; -.
DR KEGG; mmu:77371; -.
DR UCSC; uc007iui.1; mouse. [Q3U2P1-1]
DR UCSC; uc007iul.1; mouse. [Q3U2P1-2]
DR CTD; 10802; -.
DR MGI; MGI:1924621; Sec24a.
DR VEuPathDB; HostDB:ENSMUSG00000036391; -.
DR eggNOG; KOG1985; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_2_0_1; -.
DR InParanoid; Q3U2P1; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR PhylomeDB; Q3U2P1; -.
DR TreeFam; TF350406; -.
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; 77371; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Sec24a; mouse.
DR PRO; PR:Q3U2P1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3U2P1; protein.
DR Bgee; ENSMUSG00000036391; Expressed in epithelium of small intestine and 222 other tissues.
DR ExpressionAtlas; Q3U2P1; baseline and differential.
DR Genevisible; Q3U2P1; MM.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:MGI.
DR GO; GO:0032374; P:regulation of cholesterol transport; IMP:MGI.
DR CDD; cd01479; Sec24-like; 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; 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; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
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 Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..1090
FT /note="Protein transport protein Sec24A"
FT /id="PRO_0000205154"
FT REPEAT 963..1036
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT REGION 1..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..452
FT /note="Zinc finger-like"
FT COMPBIAS 17..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95486"
FT VAR_SEQ 572..592
FT /note="DVFIPMPENLLVNLNESKELV -> GMCYTQTHSTSWRIVPFRNVS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016990"
FT VAR_SEQ 593..1090
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016991"
FT CONFLICT 416
FT /note="Missing (in Ref. 1; BAE37580)"
FT /evidence="ECO:0000305"
FT CONFLICT 939
FT /note="T -> K (in Ref. 1; BAC26319)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038
FT /note="W -> R (in Ref. 1; BAC26319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1090 AA; 118782 MW; 392F9E2B4F8CF670 CRC64;
MAQPRIPAAR GAAASLQAQN GAASASGSPY TNGPVHNTLM SPQVSSSQGY DSQPPGSYPR
PMPAKTLNPF SAQSNYGGSQ GSGQTLNSPL VTSGPVLPSL HSGPVPRMPL PTSQNPAATP
MPSGSFLPGA NPPPPLNWQY NYPSTGPQTN HFPHVAPPTL PGNPNLTADH QYVSSGDPAL
QTSFKKPGSA LPLQNPPLPP TFQPGAPPGP PPAGGPPPSR GPAPQKTPPR AAPPPSFNSA
VNQEGITSNA NNGSTAAHNT YDEIEGGGFL ATPQLVNQNP KTSRSVGSAY PSLPPGYQNS
APPVAGMPPP SLSYPSGPQA FTQTPLGANH LTASMSGLSL HPEGLRVVNL LQERNMLPST
PLQPPVPNLL EDIQKLNCNP ELFRCTLTSV PQTQALLNKA KLPLGLLLHP FKDLVQLPVV
TSSTIVRCRS CRTYINPFVN FLDQRRWKCN LCYRVNDVPE EFMYNPLTRV YGEPHKRPEV
QNATIEFMAP SEYMLRPPQP PVYLFVFDVS HNAIETGYLN SVCQSLLDNL DLLPGNTRTK
IGFITFDSTI HFYSLQEGLS QPQMLIVSDI DDVFIPMPEN LLVNLNESKE LVQDLLKTLP
QMFTKTLETQ SALGPALQAA FKLISPTGGR MSVFQTQLPT LGVGALKPRE EPNQRSSAKE
IHLTPSTDFY KKLALDCSGQ QAAVDLFLLS GQYSDLASLG CISRYSAGSV YYYPSYHHQH
NPVQVQKLQK ELHRYLTRKI GFEAVMRIRC TKGLSIHTFH GNFFVRSTDL LSLPNVNPDA
GYAVQMSVEE SLTDTQLVSF QSALLYTSSK GERRIRVHTL CLPVVSTLNE VFLGADVQAI
SGLLANMAVD RSVTASLSDA RDALVNAVID SLSAYRSSVL SGQQPGLMVP FSLRLFPLFV
LALLKQKSFQ TGTSIRLDER IFAMCQVKSQ PLVHLMLTTH PSLYRVDNLS DEGALNINDR
TIPQPPILQL SVEKLSRDGA FLMDAGSLLM LWVGRNCSQN FLSQVLGVQN YASIPQTMTD
LPELDTPESA RIAAFISWLR EQRPFFPVLY VIREESLMKA AFLQSLVEDR TESALSYYEF
LLHIQQQVNK
