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GELS_MOUSE
ID   GELS_MOUSE              Reviewed;         780 AA.
AC   P13020; Q3UPB1; Q8R590;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 3.
DT   03-AUG-2022, entry version 212.
DE   RecName: Full=Gelsolin;
DE   AltName: Full=Actin-depolymerizing factor;
DE            Short=ADF;
DE   AltName: Full=Brevin;
DE   Flags: Precursor;
GN   Name=Gsn; Synonyms=Gsb;
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] (ISOFORM 2).
RX   PubMed=2546951; DOI=10.1016/s0021-9258(18)51626-4;
RA   Dieffenbach C.W., Sengupta D.N., Krause D., Sawzak D., Silverman R.H.;
RT   "Cloning of murine gelsolin and its regulation during differentiation of
RT   embryonal carcinoma cells.";
RL   J. Biol. Chem. 264:13281-13288(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
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   PROTEIN SEQUENCE OF 50-70 (ISOFORM 2), PROTEIN SEQUENCE OF 74-97; 146-160;
RP   167-186; 254-293; 301-336; 359-366; 372-388; 396-445; 456-479; 529-546;
RP   552-562; 583-621; 625-646; 667-673; 712-736 AND 739-746 (ISOFORMS 1/2),
RP   CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2), ACETYLATION AT MET-1 (ISOFORM
RP   2), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 51-73.
RC   TISSUE=Fibroblast;
RX   PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
RN   [6]
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   [7]
RP   INTERACTION WITH EIF2AK2.
RX   PubMed=22633459; DOI=10.1016/j.immuni.2012.02.020;
RA   Irving A.T., Wang D., Vasilevski O., Latchoumanin O., Kozer N.,
RA   Clayton A.H., Szczepny A., Morimoto H., Xu D., Williams B.R., Sadler A.J.;
RT   "Regulation of actin dynamics by protein kinase R control of gelsolin
RT   enforces basal innate immune defense.";
RL   Immunity 36:795-806(2012).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-582, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Calcium-regulated, actin-modulating protein that binds to the
CC       plus (or barbed) ends of actin monomers or filaments, preventing
CC       monomer exchange (end-blocking or capping). It can promote the assembly
CC       of monomers into filaments (nucleation) as well as sever filaments
CC       already formed. Plays a role in ciliogenesis.
CC   -!- SUBUNIT: Binds to actin and to fibronectin. Identified in a complex
CC       composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with
CC       the inactive form of EIF2AK2/PKR. {ECO:0000250,
CC       ECO:0000269|PubMed:22633459}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=Secreted, Plasma;
CC         IsoId=P13020-1; Sequence=Displayed;
CC       Name=2; Synonyms=Cytoplasmic;
CC         IsoId=P13020-2; Sequence=VSP_018960;
CC   -!- PTM: Phosphorylated on tyrosine residues in vitro. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR   EMBL; J04953; AAA37677.1; -; mRNA.
DR   EMBL; AK076156; BAC36223.1; -; mRNA.
DR   EMBL; AK089934; BAC41004.1; -; mRNA.
DR   EMBL; AK143664; BAE25485.1; -; mRNA.
DR   EMBL; BC023143; AAH23143.2; -; mRNA.
DR   CCDS; CCDS15960.1; -. [P13020-1]
DR   CCDS; CCDS79785.1; -. [P13020-2]
DR   RefSeq; NP_666232.2; NM_146120.4. [P13020-1]
DR   PDB; 1NPH; X-ray; 3.00 A; A=439-767.
DR   PDB; 4CBU; X-ray; 1.30 A; G=50-174.
DR   PDB; 4CBW; X-ray; 2.50 A; G=50-174.
DR   PDB; 4CBX; X-ray; 2.20 A; G=50-174.
DR   PDB; 5MVV; X-ray; 1.40 A; G=50-174.
DR   PDB; 6I4D; X-ray; 1.24 A; G=50-174.
DR   PDB; 6I4E; X-ray; 1.22 A; G=50-174.
DR   PDB; 6I4F; X-ray; 1.50 A; G=50-174.
DR   PDB; 6I4G; X-ray; 2.00 A; G/H=50-174.
DR   PDB; 6I4H; X-ray; 1.40 A; G=50-174.
DR   PDB; 6I4I; X-ray; 1.90 A; G=50-174.
DR   PDB; 6I4J; X-ray; 1.50 A; G=50-174.
DR   PDB; 6I4K; X-ray; 1.83 A; G=50-174.
DR   PDB; 6I4L; X-ray; 1.83 A; G=50-174.
DR   PDB; 6I4M; X-ray; 1.87 A; G=50-174.
DR   PDBsum; 1NPH; -.
DR   PDBsum; 4CBU; -.
DR   PDBsum; 4CBW; -.
DR   PDBsum; 4CBX; -.
DR   PDBsum; 5MVV; -.
DR   PDBsum; 6I4D; -.
DR   PDBsum; 6I4E; -.
DR   PDBsum; 6I4F; -.
DR   PDBsum; 6I4G; -.
DR   PDBsum; 6I4H; -.
DR   PDBsum; 6I4I; -.
DR   PDBsum; 6I4J; -.
DR   PDBsum; 6I4K; -.
DR   PDBsum; 6I4L; -.
DR   PDBsum; 6I4M; -.
DR   AlphaFoldDB; P13020; -.
DR   SMR; P13020; -.
DR   BioGRID; 230683; 23.
DR   CORUM; P13020; -.
DR   DIP; DIP-31941N; -.
DR   IntAct; P13020; 14.
DR   MINT; P13020; -.
DR   STRING; 10090.ENSMUSP00000028239; -.
DR   iPTMnet; P13020; -.
DR   PhosphoSitePlus; P13020; -.
DR   SwissPalm; P13020; -.
DR   REPRODUCTION-2DPAGE; P13020; -.
DR   CPTAC; non-CPTAC-3366; -.
DR   CPTAC; non-CPTAC-3514; -.
DR   EPD; P13020; -.
DR   jPOST; P13020; -.
DR   MaxQB; P13020; -.
DR   PaxDb; P13020; -.
DR   PeptideAtlas; P13020; -.
DR   PRIDE; P13020; -.
DR   ProteomicsDB; 272952; -. [P13020-1]
DR   ProteomicsDB; 272953; -. [P13020-2]
DR   Antibodypedia; 3387; 770 antibodies from 47 providers.
DR   DNASU; 227753; -.
DR   Ensembl; ENSMUST00000028239; ENSMUSP00000028239; ENSMUSG00000026879. [P13020-1]
DR   Ensembl; ENSMUST00000201185; ENSMUSP00000144561; ENSMUSG00000026879. [P13020-2]
DR   GeneID; 227753; -.
DR   KEGG; mmu:227753; -.
DR   UCSC; uc008jkc.2; mouse. [P13020-1]
DR   CTD; 2934; -.
DR   MGI; MGI:95851; Gsn.
DR   VEuPathDB; HostDB:ENSMUSG00000026879; -.
DR   eggNOG; KOG0443; Eukaryota.
DR   GeneTree; ENSGT00940000155591; -.
DR   InParanoid; P13020; -.
DR   OMA; DNRTKTH; -.
DR   PhylomeDB; P13020; -.
DR   TreeFam; TF313468; -.
DR   Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 227753; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Gsn; mouse.
DR   EvolutionaryTrace; P13020; -.
DR   PRO; PR:P13020; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P13020; protein.
DR   Bgee; ENSMUSG00000026879; Expressed in skin of external ear and 293 other tissues.
DR   ExpressionAtlas; P13020; baseline and differential.
DR   Genevisible; P13020; MM.
DR   GO; GO:0030478; C:actin cap; ISO:MGI.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0002102; C:podosome; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0001726; C:ruffle; ISO:MGI.
DR   GO; GO:0016528; C:sarcoplasm; ISO:MGI.
DR   GO; GO:0003779; F:actin binding; ISO:MGI.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0045159; F:myosin II binding; ISO:MGI.
DR   GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IPI:BHF-UCL.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:BHF-UCL.
DR   GO; GO:0051693; P:actin filament capping; IDA:UniProtKB.
DR   GO; GO:0030042; P:actin filament depolymerization; IMP:BHF-UCL.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR   GO; GO:0090527; P:actin filament reorganization; ISO:MGI.
DR   GO; GO:0051014; P:actin filament severing; IMP:UniProtKB.
DR   GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; ISO:MGI.
DR   GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0086003; P:cardiac muscle cell contraction; IMP:BHF-UCL.
DR   GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR   GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0097284; P:hepatocyte apoptotic process; ISO:MGI.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR   GO; GO:0051127; P:positive regulation of actin nucleation; ISO:MGI.
DR   GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; ISO:MGI.
DR   GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; IMP:UniProtKB.
DR   GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR   GO; GO:1903903; P:regulation of establishment of T cell polarity; ISO:MGI.
DR   GO; GO:1903906; P:regulation of plasma membrane raft polarization; ISO:MGI.
DR   GO; GO:0071801; P:regulation of podosome assembly; ISO:MGI.
DR   GO; GO:1903909; P:regulation of receptor clustering; ISO:MGI.
DR   GO; GO:0055119; P:relaxation of cardiac muscle; IMP:BHF-UCL.
DR   GO; GO:0097017; P:renal protein absorption; ISO:MGI.
DR   GO; GO:0035994; P:response to muscle stretch; IMP:BHF-UCL.
DR   GO; GO:0042989; P:sequestering of actin monomers; ISO:MGI.
DR   GO; GO:0014891; P:striated muscle atrophy; ISO:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:MGI.
DR   Gene3D; 3.40.20.10; -; 6.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR030004; Gelsolin.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   PANTHER; PTHR11977; PTHR11977; 1.
DR   PANTHER; PTHR11977:SF27; PTHR11977:SF27; 1.
DR   Pfam; PF00626; Gelsolin; 6.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Alternative initiation; Calcium; Cilium biogenesis/degradation; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..780
FT                   /note="Gelsolin"
FT                   /id="PRO_0000036387"
FT   REPEAT          74..124
FT                   /note="Gelsolin-like 1"
FT   REPEAT          196..236
FT                   /note="Gelsolin-like 2"
FT   REPEAT          312..354
FT                   /note="Gelsolin-like 3"
FT   REPEAT          451..502
FT                   /note="Gelsolin-like 4"
FT   REPEAT          574..614
FT                   /note="Gelsolin-like 5"
FT   REPEAT          677..719
FT                   /note="Gelsolin-like 6"
FT   REGION          51..174
FT                   /note="Actin-severing"
FT                   /evidence="ECO:0000255"
FT   REGION          121..124
FT                   /note="Actin-actin interfilament contact point"
FT   REGION          244..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..780
FT                   /note="Actin-binding, Ca-sensitive"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        244..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160..167
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..194
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         549
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         589
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         590
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         612
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         694
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         695
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         717
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         84
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   MOD_RES         407
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   MOD_RES         463
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   MOD_RES         582
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         601
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   MOD_RES         649
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   MOD_RES         740
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P06396"
FT   DISULFID        213..226
FT                   /note="In isoform 1"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..49
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:2546951"
FT                   /id="VSP_018960"
FT   CONFLICT        262..263
FT                   /note="GG -> ET (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="P -> H (in Ref. 2; BAC41004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="R -> K (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="E -> K (in Ref. 2; BAC41004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="A -> P (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="A -> G (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615
FT                   /note="G -> A (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="A -> G (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="A -> S (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        763
FT                   /note="D -> N (in Ref. 1; AAA37677)"
FT                   /evidence="ECO:0000305"
FT   HELIX           55..59
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          62..72
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          92..100
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          106..114
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   HELIX           120..136
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          164..167
FT                   /evidence="ECO:0007829|PDB:6I4E"
FT   STRAND          445..451
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          454..457
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           460..462
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          465..467
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          470..477
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          486..492
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           498..514
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   TURN            515..517
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          519..525
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           531..535
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   TURN            536..539
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          542..546
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          551..553
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          560..568
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          570..572
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          574..579
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           583..585
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          590..595
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          600..604
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           610..623
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          627..631
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           637..643
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           653..656
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           660..662
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          666..671
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          674..676
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          678..681
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           688..690
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          695..700
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          705..709
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           715..729
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   TURN            733..735
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   STRAND          742..746
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   HELIX           752..755
FT                   /evidence="ECO:0007829|PDB:1NPH"
FT   INIT_MET        P13020-2:1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000269|Ref.4"
FT   MOD_RES         P13020-2:1
FT                   /note="N-acetylmethionine; alternate"
FT                   /evidence="ECO:0000269|Ref.4"
SQ   SEQUENCE   780 AA;  85942 MW;  AE94297BE457FF2D CRC64;
     MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM VVEHPEFLKA
     GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ LRNGNLQYDL HYWLGNECSQ
     DESGAAAIFT VQLDDYLNGR AVQHREVQGF ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN
     EVVVQRLFQV KGRRVVRATE VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ
     VSKGIRDNER SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK
     VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM EERKAALKTA
     SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT DGPGLGYLSS HIANVERVPF
     DAATLHTSTA MAAQHGMDDD GTGQKQIWRI EGSNKVPVDP ATYGQFYGGD SYIILYNYRH
     GGRQGQIIYN WQGAQSTQDE VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK
     PMIIYKGGTS RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA
     YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW EALGGKTAYR TSPRLKDKKM
     DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD TWDQVFVWVG KDSQEEEKTE
     ALTSAKRYIE TDPANRDRRT PITVVRQGFE PPSFVGWFLG WDDNYWSVDP LDRALAELAA
 
 
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