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Protein transport protein Sec24A (SEC24-related protein A)

 SC24A_HUMAN             Reviewed;        1093 AA.
O95486; A8MVW3; Q8WUV2; Q96GP7;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
07-APR-2021, entry version 183.
RecName: Full=Protein transport protein Sec24A {ECO:0000305};
AltName: Full=SEC24-related protein A;
Name=SEC24A {ECO:0000312|HGNC:HGNC:10703};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 690-1093 (ISOFORM 1), AND VARIANTS ILE-302 AND
MET-396.
TISSUE=Brain, and Eye;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-1093 (ISOFORM 1).
TISSUE=B-cell;
PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L.,
Paccaud J.-P.;
"Sec24 proteins and sorting at the endoplasmic reticulum.";
J. Biol. Chem. 274:7833-7840(1999).
[4]
FUNCTION, AND INTERACTION WITH TMED2.
PubMed=20427317; DOI=10.1242/jcs.062950;
Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
"Selective export of human GPI-anchored proteins from the endoplasmic
reticulum.";
J. Cell Sci. 123:1705-1715(2010).
[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]
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).
[7]
INTERACTION WITH TMEM39A AND SACM1L.
PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
Miao G., Zhang Y., Chen D., Zhang H.;
"The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
Mol. Cell 0:0-0(2019).
[8] {ECO:0007744|PDB:2NUP, ECO:0007744|PDB:2NUT}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 341-1093 IN COMPLEX WITH ZINC;
SEC23A AND SEC22B, FUNCTION, INTERACTION WITH SEC22B, SUBUNIT, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF ARG-541.
PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
Mancias J.D., Goldberg J.;
"The transport signal on Sec22 for packaging into COPII-coated vesicles is
a conformational epitope.";
Mol. Cell 26:403-414(2007).
[9] {ECO:0007744|PDB:3EGD, ECO:0007744|PDB:3EGX}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 346-1093 IN COMPLEX WITH CARGO
PEPTIDES; SEC22B; SEC23A AND ZINC, AND FUNCTION.
PubMed=18843296; DOI=10.1038/emboj.2008.208;
Mancias J.D., Goldberg J.;
"Structural basis of cargo membrane protein discrimination by the human
COPII coat machinery.";
EMBO J. 27:2918-2928(2008).
[10]
INTERACTION WITH STING1.
PubMed=32690950; DOI=10.1038/s41590-020-0730-5;
Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
Thomsen M.K., Paludan S.R.;
"STEEP mediates STING ER exit and activation of signaling.";
Nat. Immunol. 21:868-879(2020).
[11]
ERRATUM OF PUBMED:32690950.
PubMed=32929276; DOI=10.1038/s41590-020-0803-5;
Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
Thomsen M.K., Paludan S.R.;
Nat. Immunol. 21:1468-1469(2020).
-!- 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
(PubMed:20427317, PubMed:17499046, PubMed:18843296). Plays a central
role in cargo selection within the COPII complex and together with
SEC24B may have a different specificity compared to SEC24C and SEC24D.
May package preferentially cargos with cytoplasmic DxE or LxxLE motifs
and may also recognize conformational epitopes (PubMed:17499046,
PubMed:18843296). {ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
-!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
complex, the Sec13/31 complex and Sar1 (PubMed:17499046). Interacts
with TMED2 (PubMed:20427317). Interacts (as part of the Sec23/24
complex) with SEC22B; recruits SEC22B into COPII-coated vesicles for
its transport from the endoplasmic reticulum to the Golgi
(PubMed:17499046). Interacts with STING1; promoting STING1
translocation to COPII vesicles in a STEEP1-dependent manner
(PubMed:32690950). Interacts with TMEM39A (PubMed:31806350). Interacts
with SACM1L; this interaction is reduced in the absence of TMEM39A
(PubMed:31806350). {ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:31806350,
ECO:0000269|PubMed:32690950}.
-!- INTERACTION:
O95486; Q01844: EWSR1; NbExp=3; IntAct=EBI-749911, EBI-739737;
O95486; Q92734: TFG; NbExp=3; IntAct=EBI-749911, EBI-357061;
O95486-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-12320085, EBI-948603;
O95486-2; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-12320085, EBI-724639;
O95486-2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-12320085, EBI-11975223;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000305|PubMed:17499046}; Peripheral membrane protein
{ECO:0000305|PubMed:17499046}; Cytoplasmic side
{ECO:0000305|PubMed:17499046}. Endoplasmic reticulum membrane
{ECO:0000305|PubMed:17499046}; Peripheral membrane protein
{ECO:0000305|PubMed:17499046}; Cytoplasmic side
{ECO:0000305|PubMed:17499046}. Cytoplasm, cytosol
{ECO:0000305|PubMed:17499046}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95486-1; Sequence=Displayed;
Name=2;
IsoId=O95486-2; Sequence=VSP_029571, VSP_029572;
-!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA10334.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=COPII entry;
URL="https://en.wikipedia.org/wiki/COPII";
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EMBL; CH471062; EAW62246.1; -; Genomic_DNA.
EMBL; BC009325; AAH09325.2; -; mRNA.
EMBL; BC019341; AAH19341.1; -; mRNA.
EMBL; AJ131244; CAA10334.1; ALT_FRAME; mRNA.
CCDS; CCDS43363.1; -. [O95486-1]
CCDS; CCDS58967.1; -. [O95486-2]
RefSeq; NP_001239160.1; NM_001252231.1. [O95486-2]
RefSeq; NP_068817.1; NM_021982.2. [O95486-1]
PDB; 2NUP; X-ray; 2.80 A; B=341-1093.
PDB; 2NUT; X-ray; 2.30 A; B=341-1093.
PDB; 3EGD; X-ray; 2.70 A; B=346-1093.
PDB; 3EGX; X-ray; 3.30 A; B=346-1093.
PDB; 5VNE; X-ray; 2.70 A; B=346-1093.
PDB; 5VNF; X-ray; 2.41 A; B=346-1093.
PDB; 5VNG; X-ray; 2.60 A; B=346-1093.
PDB; 5VNH; X-ray; 2.60 A; B=346-1093.
PDB; 5VNI; X-ray; 2.79 A; B=346-1093.
PDB; 5VNJ; X-ray; 2.81 A; B=346-1093.
PDB; 5VNK; X-ray; 2.55 A; B=346-1093.
PDB; 5VNL; X-ray; 2.39 A; B=346-1093.
PDB; 5VNM; X-ray; 2.77 A; B=346-1093.
PDB; 5VNN; X-ray; 2.50 A; B=346-1093.
PDB; 5VNO; X-ray; 2.90 A; B=346-1093.
PDBsum; 2NUP; -.
PDBsum; 2NUT; -.
PDBsum; 3EGD; -.
PDBsum; 3EGX; -.
PDBsum; 5VNE; -.
PDBsum; 5VNF; -.
PDBsum; 5VNG; -.
PDBsum; 5VNH; -.
PDBsum; 5VNI; -.
PDBsum; 5VNJ; -.
PDBsum; 5VNK; -.
PDBsum; 5VNL; -.
PDBsum; 5VNM; -.
PDBsum; 5VNN; -.
PDBsum; 5VNO; -.
SMR; O95486; -.
BioGRID; 116016; 122.
IntAct; O95486; 25.
STRING; 9606.ENSP00000381823; -.
iPTMnet; O95486; -.
MetOSite; O95486; -.
PhosphoSitePlus; O95486; -.
BioMuta; SEC24A; -.
EPD; O95486; -.
jPOST; O95486; -.
MassIVE; O95486; -.
MaxQB; O95486; -.
PaxDb; O95486; -.
PeptideAtlas; O95486; -.
PRIDE; O95486; -.
ProteomicsDB; 50913; -. [O95486-1]
ProteomicsDB; 50914; -. [O95486-2]
Antibodypedia; 45232; 105 antibodies.
Ensembl; ENST00000322887; ENSP00000321749; ENSG00000113615. [O95486-2]
Ensembl; ENST00000398844; ENSP00000381823; ENSG00000113615. [O95486-1]
GeneID; 10802; -.
KEGG; hsa:10802; -.
UCSC; uc003kzs.4; human. [O95486-1]
CTD; 10802; -.
GeneCards; SEC24A; -.
HGNC; HGNC:10703; SEC24A.
HPA; ENSG00000113615; Low tissue specificity.
MIM; 607183; gene.
neXtProt; NX_O95486; -.
OpenTargets; ENSG00000113615; -.
PharmGKB; PA35626; -.
VEuPathDB; HostDB:ENSG00000113615.12; -.
eggNOG; KOG1985; Eukaryota.
GeneTree; ENSGT00950000182924; -.
HOGENOM; CLU_004589_2_0_1; -.
InParanoid; O95486; -.
OMA; VVQDQVI; -.
PhylomeDB; O95486; -.
TreeFam; TF350406; -.
PathwayCommons; O95486; -.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
BioGRID-ORCS; 10802; 10 hits in 988 CRISPR screens.
ChiTaRS; SEC24A; human.
EvolutionaryTrace; O95486; -.
GenomeRNAi; 10802; -.
Pharos; O95486; Tbio.
PRO; PR:O95486; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; O95486; protein.
Bgee; ENSG00000113615; Expressed in jejunal mucosa and 242 other tissues.
ExpressionAtlas; O95486; baseline and differential.
Genevisible; O95486; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
CDD; cd01479; Sec24-like; 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; 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; IPR041742; Sec24-like_trunk_dom.
InterPro; IPR036465; vWFA_dom_sf.
InterPro; IPR006895; Znf_Sec23_Sec24.
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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
Protein transport; Reference proteome; Transport; Zinc.
CHAIN 1..1093
/note="Protein transport protein Sec24A"
/id="PRO_0000205153"
REPEAT 966..1038
/note="Gelsolin-like"
/evidence="ECO:0000255"
REGION 431..455
/note="Zinc finger-like"
COMPBIAS 89..237
/note="Pro-rich"
METAL 431
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
METAL 434
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
METAL 452
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
METAL 455
/note="Zinc"
/evidence="ECO:0007744|PDB:2NUP, ECO:0007744|PDB:3EGD"
VAR_SEQ 594..613
/note="LVQDLLKTLPQMFTKTLETQ -> SVIGVSSEETLITCLEIAMR (in
isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_029571"
VAR_SEQ 614..1093
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_029572"
VARIANT 261
/note="S -> G (in dbSNP:rs7718102)"
/id="VAR_037253"
VARIANT 302
/note="T -> I (in dbSNP:rs17851746)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_037254"
VARIANT 396
/note="T -> M (in dbSNP:rs17851745)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_037255"
MUTAGEN 541
/note="R->A: Decreased ability to interact with and package
the SNARE SEC22B cargo into COPII vesicles. Has no effect
on other cargos packaging."
/evidence="ECO:0000269|PubMed:17499046"
STRAND 350..352
/evidence="ECO:0007744|PDB:2NUT"
HELIX 353..356
/evidence="ECO:0007744|PDB:2NUT"
HELIX 374..377
/evidence="ECO:0007744|PDB:2NUT"
TURN 383..385
/evidence="ECO:0007744|PDB:2NUT"
STRAND 386..396
/evidence="ECO:0007744|PDB:2NUT"
HELIX 397..403
/evidence="ECO:0007744|PDB:2NUT"
STRAND 408..411
/evidence="ECO:0007744|PDB:2NUT"
TURN 432..434
/evidence="ECO:0007744|PDB:2NUT"
STRAND 442..451
/evidence="ECO:0007744|PDB:2NUT"
TURN 453..455
/evidence="ECO:0007744|PDB:2NUT"
STRAND 458..460
/evidence="ECO:0007744|PDB:2NUT"
HELIX 463..465
/evidence="ECO:0007744|PDB:5VNJ"
HELIX 477..479
/evidence="ECO:0007744|PDB:2NUT"
HELIX 481..484
/evidence="ECO:0007744|PDB:2NUT"
STRAND 486..491
/evidence="ECO:0007744|PDB:2NUT"
HELIX 494..496
/evidence="ECO:0007744|PDB:2NUT"
STRAND 498..500
/evidence="ECO:0007744|PDB:2NUT"
STRAND 505..511
/evidence="ECO:0007744|PDB:2NUT"
HELIX 514..519
/evidence="ECO:0007744|PDB:2NUT"
HELIX 521..532
/evidence="ECO:0007744|PDB:2NUT"
TURN 533..535
/evidence="ECO:0007744|PDB:2NUT"
STRAND 543..557
/evidence="ECO:0007744|PDB:2NUT"
STRAND 562..564
/evidence="ECO:0007744|PDB:2NUT"
STRAND 566..570
/evidence="ECO:0007744|PDB:2NUT"
HELIX 573..575
/evidence="ECO:0007744|PDB:5VNI"
STRAND 581..587
/evidence="ECO:0007744|PDB:2NUT"
TURN 588..591
/evidence="ECO:0007744|PDB:2NUT"
HELIX 592..601
/evidence="ECO:0007744|PDB:2NUT"
HELIX 602..604
/evidence="ECO:0007744|PDB:2NUT"
TURN 605..608
/evidence="ECO:0007744|PDB:2NUT"
HELIX 616..627
/evidence="ECO:0007744|PDB:2NUT"
TURN 628..630
/evidence="ECO:0007744|PDB:2NUT"
STRAND 632..638
/evidence="ECO:0007744|PDB:2NUT"
STRAND 657..659
/evidence="ECO:0007744|PDB:2NUP"
HELIX 672..682
/evidence="ECO:0007744|PDB:2NUT"
STRAND 685..691
/evidence="ECO:0007744|PDB:2NUT"
HELIX 699..702
/evidence="ECO:0007744|PDB:2NUT"
HELIX 704..707
/evidence="ECO:0007744|PDB:2NUT"
TURN 708..710
/evidence="ECO:0007744|PDB:2NUT"
STRAND 713..715
/evidence="ECO:0007744|PDB:2NUT"
TURN 721..723
/evidence="ECO:0007744|PDB:2NUT"
HELIX 725..740
/evidence="ECO:0007744|PDB:2NUT"
STRAND 744..753
/evidence="ECO:0007744|PDB:2NUT"
STRAND 757..768
/evidence="ECO:0007744|PDB:2NUT"
STRAND 770..772
/evidence="ECO:0007744|PDB:5VNL"
STRAND 774..779
/evidence="ECO:0007744|PDB:2NUT"
STRAND 785..793
/evidence="ECO:0007744|PDB:2NUT"
STRAND 799..810
/evidence="ECO:0007744|PDB:2NUT"
STRAND 816..828
/evidence="ECO:0007744|PDB:2NUT"
HELIX 831..836
/evidence="ECO:0007744|PDB:2NUT"
HELIX 840..857
/evidence="ECO:0007744|PDB:2NUT"
HELIX 860..879
/evidence="ECO:0007744|PDB:2NUT"
STRAND 891..893
/evidence="ECO:0007744|PDB:2NUT"
HELIX 894..896
/evidence="ECO:0007744|PDB:2NUT"
HELIX 899..908
/evidence="ECO:0007744|PDB:2NUT"
TURN 910..912
/evidence="ECO:0007744|PDB:2NUT"
HELIX 920..932
/evidence="ECO:0007744|PDB:2NUT"
HELIX 935..942
/evidence="ECO:0007744|PDB:2NUT"
STRAND 945..948
/evidence="ECO:0007744|PDB:2NUT"
STRAND 954..956
/evidence="ECO:0007744|PDB:2NUT"
STRAND 960..962
/evidence="ECO:0007744|PDB:5VNE"
TURN 975..977
/evidence="ECO:0007744|PDB:2NUT"
STRAND 982..987
/evidence="ECO:0007744|PDB:2NUT"
STRAND 989..996
/evidence="ECO:0007744|PDB:2NUT"
HELIX 1002..1007
/evidence="ECO:0007744|PDB:2NUT"
HELIX 1014..1016
/evidence="ECO:0007744|PDB:2NUT"
HELIX 1030..1043
/evidence="ECO:0007744|PDB:2NUT"
STRAND 1046..1048
/evidence="ECO:0007744|PDB:2NUT"
STRAND 1051..1053
/evidence="ECO:0007744|PDB:2NUT"
STRAND 1058..1061
/evidence="ECO:0007744|PDB:2NUT"
HELIX 1066..1068
/evidence="ECO:0007744|PDB:2NUT"
STRAND 1075..1077
/evidence="ECO:0007744|PDB:5VNH"
HELIX 1080..1091
/evidence="ECO:0007744|PDB:2NUT"
SEQUENCE 1093 AA; 119749 MW; E21F3A1333674A6A CRC64;
MSQPGIPASG GAPASLQAQN GAALASGSPY TNGPVQNALL SSQESVSQGY NFQLPGSYPH
PIPAKTLNPV SGQSNYGGSQ GSGQTLNRPP VASNPVTPSL HSGPAPRMPL PASQNPATTP
MPSSSFLPEA NLPPPLNWQY NYPSTASQTN HCPRASSQPT VSGNTSLTTN HQYVSSGYPS
LQNSFIKSGP SVPPLVNPPL PTTFQPGAPH GPPPAGGPPP VRALTPLTSS YRDVPQPLFN
SAVNQEGITS NTNNGSMVVH SSYDEIEGGG LLATPQLTNK NPKMSRSVGY SYPSLPPGYQ
NTTPPGATGV PPSSLNYPSG PQAFTQTPLG ANHLTTSMSG LSLQPEGLRV VNLLQERNML
PSTPLKPPVP NLHEDIQKLN CNPELFRCTL TSIPQTQALL NKAKLPLGLL LHPFKDLVQL
PVVTSSTIVR CRSCRTYINP FVSFLDQRRW KCNLCYRVND VPEEFLYNPL TRVYGEPHRR
PEVQNATIEF MAPSEYMLRP PQPPVYLFVF DVSHNAVETG YLNSVCQSLL DNLDLLPGNT
RTKIGFITFD STIHFYGLQE SLSQPQMLIV SDIEDVFIPM PENLLVNLNE SKELVQDLLK
TLPQMFTKTL ETQSALGPAL QAAFKLMSPT GGRMSVFQTQ LPTLGVGALK PREEPNHRSS
AKDIHMTPST DFYKKLALDC SGQQVAVDLF LLSGQYSDLA SLGCISRYSA GSVYYYPSYH
HQHNPVQVQK LQKELQRYLT RKIGFEAVMR IRCTKGLSIH TFHGNFFVRS TDLLSLPNVN
PDAGYAVQMS VEESLTDTQL VSFQSALLYT SSKGERRIRV HTLCLPVVST LNDVFLGADV
QAISGLLANM AVDRSMTASL SDARDALVNA VIDSLSAYRS SVLSNQQPGL MVPFSLRLFP
LFVLALLKQK SFQTGTNARL DERIFAMCQV KNQPLVYLML TTHPSLYRVD NLSDEGALNI
SDRTIPQPPI LQLSVEKLSR DGAFLMDAGS VLMLWVGKNC TQNFLSQVLG VQNYASIPQP
MTDLPELDTP ESARIIAFIS WLREQRPFFP ILYVIRDESP MKANFLQNMI EDRTESALSY
YEFLLHIQQQ VNK


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Related Genes :
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[Sec24a] Protein transport protein Sec24A (SEC24-related protein A)
[SEC24B] Protein transport protein Sec24B (SEC24-related protein B)
[SEC24A] Protein transport protein Sec24A (SEC24-related protein A)
[SEC24 ANU1 YIL109C] Protein transport protein SEC24 (Abnormal nuclear morphology 1)
[YIPF5 FINGER5 YIP1A PP12723 SB140 UNQ3123/PRO10275] Protein YIPF5 (Five-pass transmembrane protein localizing in the Golgi apparatus and the endoplasmic reticulum 5) (Smooth muscle cell-associated protein 5) (SMAP-5) (YIP1 family member 5) (YPT-interacting protein 1 A)
[TMED2 RNP24] Transmembrane emp24 domain-containing protein 2 (Membrane protein p24A) (p24) (p24 family protein beta-1) (p24beta1)
[Tmed2 Rnp24] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (RNP21.4) (p24 family protein beta-1) (p24beta1)
[Tmed2 Rnp24 Sid394] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (Sid 394) (p24 family protein beta-1) (p24beta1)
[SEC22B SEC22L1] Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1)
[PEF1 ABP32 UNQ1845/PRO3573] Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1)
[STING1 ERIS MITA TMEM173] Stimulator of interferon genes protein (hSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (hMITA) (Transmembrane protein 173)
[TMEM39A SUSR2] Transmembrane protein 39A
[SEC23B] Protein transport protein Sec23B (hSec23B) (SEC23-related protein B)
[Sting1 Eris Mita Mpys Tmem173] Stimulator of interferon genes protein (mSTING) (Endoplasmic reticulum interferon stimulator) (ERIS) (Mediator of IRF3 activation) (MMITA) (Transmembrane protein 173)
[Sting1 Tmem173] Stimulator of interferon genes protein (rSTING) (Transmembrane protein 173)
[STING1 TMEM173] Stimulator of interferon genes protein (STING) (Transmembrane protein 173)
[STING1 TMEM173] Stimulator of interferon genes protein (poSTING) (Transmembrane protein 173)
[SACM1L KIAA0851 SAC1] Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein)
[TFG] Protein TFG (TRK-fused gene protein)
[EWSR1 EWS] RNA-binding protein EWS (EWS oncogene) (Ewing sarcoma breakpoint region 1 protein)
[sec24 NCU02391] Protein transport protein sec24
[Sec22b Sec22l1] Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) (mSec22b)
[Sec22b Sec22l1] Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1)
[Yipf5 Yip1a] Protein YIPF5 (YIP1 family member 5) (YPT-interacting protein 1 A)
[Sacm1l Sac1] Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein)
[TMED2 RNP24] Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (p24 family protein beta-1) (p24beta1) (Fragment)
[SEC13 ANU3 YLR208W L8167.4] Protein transport protein SEC13
[SAR1 YPL218W] Small COPII coat GTPase SAR1 (EC 3.6.5.-) (GTP-binding protein SAR1) (Secretion-associated RAS-related protein 1)
[Yipf5 Yip1a] Protein YIPF5 (YIP1 family member 5) (YPT-interacting protein 1 A)

Bibliography :