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DOC10_MOUSE
ID   DOC10_MOUSE             Reviewed;        2150 AA.
AC   Q8BZN6; F1AHI9;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Dedicator of cytokinesis protein 10 {ECO:0000305};
DE   AltName: Full=Zizimin-3;
GN   Name=Dock10 {ECO:0000312|MGI:MGI:2146320}; Synonyms=Kiaa0694, Ziz3;
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 4), TISSUE SPECIFICITY, AND INDUCTION
RP   BY IL4.
RC   STRAIN=BALB/cJ; TISSUE=Spleen;
RX   PubMed=21514340; DOI=10.1016/j.humimm.2011.03.024;
RA   Alcaraz-Garcia M.J., Ruiz-Lafuente N., Sebastian-Ruiz S., Majado M.J.,
RA   Gonzalez-Garcia C., Bernardo M.V., Alvarez-Lopez M.R., Parrado A.;
RT   "Human and mouse DOCK10 splicing isoforms with alternative first coding
RT   exon usage are differentially expressed in T and B lymphocytes.";
RL   Hum. Immunol. 72:531-537(2011).
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 348-2150 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1690-2150 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15710388; DOI=10.1016/j.febslet.2005.01.006;
RA   Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A., Maruyama M.;
RT   "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange
RT   factor expressed predominantly in lymphocytes.";
RL   FEBS Lett. 579:1039-1046(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877; SER-1251; SER-1257;
RP   SER-1292; SER-1295 AND THR-1440, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196; SER-302; THR-368;
RP   SER-1257; SER-1292; SER-1295; SER-1318 AND THR-1406, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, and Spleen;
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   [8]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=25729399; DOI=10.1186/s12979-015-0028-x;
RA   Matsuda T., Yanase S., Takaoka A., Maruyama M.;
RT   "The immunosenescence-related gene Zizimin2 is associated with early bone
RT   marrow B cell development and marginal zone B cell formation.";
RL   Immun. Ageing 12:1-1(2015).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP   AND DOMAIN.
RX   PubMed=25851601; DOI=10.1091/mbc.e14-08-1310;
RA   Jaudon F., Raynaud F., Wehrle R., Bellanger J.M., Doulazmi M., Vodjdani G.,
RA   Gasman S., Fagni L., Dusart I., Debant A., Schmidt S.;
RT   "The RhoGEF DOCK10 is essential for dendritic spine morphogenesis.";
RL   Mol. Biol. Cell 26:2112-2127(2015).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27502165; DOI=10.1016/j.imbio.2016.07.015;
RA   Garcia-Serna A.M., Alcaraz-Garcia M.J., Ruiz-Lafuente N.,
RA   Sebastian-Ruiz S., Martinez C.M., Moya-Quiles M.R., Minguela A.,
RA   Garcia-Alonso A.M., Martin-Orozco E., Parrado A.;
RT   "Dock10 regulates CD23 expression and sustains B-cell lymphopoiesis in
RT   secondary lymphoid tissue.";
RL   Immunobiology 221:1343-1350(2016).
CC   -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC       and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic
CC       spine morphogenesis in Purkinje cells and in hippocampal neurons, via a
CC       CDC42-mediated pathway (PubMed:25851601). Sustains B-cell lymphopoiesis
CC       in secondary lymphoid tissues and regulates FCER2/CD23 expression
CC       (PubMed:27502165). {ECO:0000269|PubMed:25851601,
CC       ECO:0000269|PubMed:27502165}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BY6}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q96BY6}. Cell projection, dendritic spine
CC       {ECO:0000269|PubMed:25851601}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=DOCK10.1 {ECO:0000303|PubMed:21514340};
CC         IsoId=Q8BZN6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZN6-2; Sequence=VSP_007718, VSP_022288;
CC       Name=3;
CC         IsoId=Q8BZN6-3; Sequence=VSP_007718, VSP_022227;
CC       Name=4; Synonyms=DOCK10.2 {ECO:0000303|PubMed:21514340};
CC         IsoId=Q8BZN6-4; Sequence=VSP_058821, VSP_058822;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, spleen, mesenteric lymph
CC       nodes (MLN) and thymus (PubMed:15710388, PubMed:25729399). Expressed by
CC       B and T splenocytes (PubMed:21514340). In brain, expressed by Purkinje
CC       cells during postnatal development and hippocampal neurons
CC       (PubMed:25851601). {ECO:0000269|PubMed:15710388,
CC       ECO:0000269|PubMed:21514340, ECO:0000269|PubMed:25729399,
CC       ECO:0000269|PubMed:25851601}.
CC   -!- DEVELOPMENTAL STAGE: At early postnatal stages, expressed broadly in
CC       the cerebellum and from P15 the expression becomes restricted to
CC       Purkinje cells. {ECO:0000269|PubMed:25851601}.
CC   -!- INDUCTION: Isoform 4 (but not isoform 1) is highly induced by IL4 in B
CC       splenocytes, but not T splenocytes. {ECO:0000269|PubMed:21514340}.
CC   -!- DOMAIN: The DOCKER domain may mediate some GEF activity.
CC       {ECO:0000269|PubMed:25851601}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice are viable and fertile
CC       (PubMed:25729399, PubMed:27502165). They show decreased numbers of B-
CC       cells in spleen, both follicular B-cells and marginal zone B-cells, and
CC       in peripheral blood, but not in bone marrow (PubMed:25729399,
CC       PubMed:27502165). Their percentage of splenic CD8(+) T-cells is
CC       decreased comparing to wild types (PubMed:25729399).
CC       {ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:27502165}.
CC   -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00983}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28567.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; GU797481; ADK73961.1; -; mRNA.
DR   EMBL; AC124672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK122347; BAC65629.1; -; mRNA.
DR   EMBL; AK034064; BAC28567.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001272856.1; NM_001285927.1.
DR   RefSeq; NP_780500.2; NM_175291.4.
DR   AlphaFoldDB; Q8BZN6; -.
DR   SMR; Q8BZN6; -.
DR   BioGRID; 229145; 6.
DR   IntAct; Q8BZN6; 4.
DR   MINT; Q8BZN6; -.
DR   STRING; 10090.ENSMUSP00000077099; -.
DR   iPTMnet; Q8BZN6; -.
DR   PhosphoSitePlus; Q8BZN6; -.
DR   SwissPalm; Q8BZN6; -.
DR   EPD; Q8BZN6; -.
DR   jPOST; Q8BZN6; -.
DR   MaxQB; Q8BZN6; -.
DR   PaxDb; Q8BZN6; -.
DR   PeptideAtlas; Q8BZN6; -.
DR   PRIDE; Q8BZN6; -.
DR   ProteomicsDB; 279750; -. [Q8BZN6-1]
DR   ProteomicsDB; 279751; -. [Q8BZN6-2]
DR   ProteomicsDB; 279752; -. [Q8BZN6-3]
DR   ProteomicsDB; 279753; -. [Q8BZN6-4]
DR   GeneID; 210293; -.
DR   KEGG; mmu:210293; -.
DR   UCSC; uc007brf.1; mouse. [Q8BZN6-2]
DR   CTD; 55619; -.
DR   MGI; MGI:2146320; Dock10.
DR   eggNOG; KOG1997; Eukaryota.
DR   InParanoid; Q8BZN6; -.
DR   OrthoDB; 20156at2759; -.
DR   PhylomeDB; Q8BZN6; -.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR   Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR   Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 210293; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Dock10; mouse.
DR   PRO; PR:Q8BZN6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8BZN6; protein.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR   GO; GO:0001782; P:B cell homeostasis; IMP:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
DR   GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08697; C2_Dock-D; 1.
DR   Gene3D; 1.20.58.740; -; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR037809; C2_Dock-D.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR021816; DOCK_C/D_N.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR043162; DOCK_C_lobe_C.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23317; PTHR23317; 1.
DR   Pfam; PF06920; DHR-2; 2.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF11878; DUF3398; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Nucleus; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   CHAIN           1..2150
FT                   /note="Dedicator of cytokinesis protein 10"
FT                   /id="PRO_0000190003"
FT   DOMAIN          181..290
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          672..850
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT   DOMAIN          1690..2150
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT   REGION          141..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         368
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         834
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BY6"
FT   MOD_RES         877
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         1232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BY6"
FT   MOD_RES         1251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         1257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1406
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1440
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   VAR_SEQ         1..42
FT                   /note="MAGERTRRFTRSLLRPGQAAELRHSAASAAAVAVSSRQQQRQ -> MSFRGK
FT                   EFWKRRRTVKRVNPEGIHKAGAQ (in isoform 4)"
FT                   /id="VSP_058821"
FT   VAR_SEQ         1739..1771
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12693553,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007718"
FT   VAR_SEQ         2150
FT                   /note="Q -> LCRGPCLYSFCASVSSISLSTVSKSDYGQGRPSKVRSGATLHHTCNQ
FT                   GDRGCTCGLHLIQCGGLRGTLEHPMHLSENSLNVLQLISGKKKIDLIYLKFLQCSCLPC
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_022288"
FT   VAR_SEQ         2150
FT                   /note="Q -> LCRGPCLYSFCASVSSISLSTVSKSGTSFSLYVYPVLQPPVHPPLLI
FT                   TSPVPQSALVAQLLLRLHCHLKTRHVDSLAFKKKTHAPSSPKCIFELFQFFKTKTQNVF
FT                   MILQNIKEKHRPGVEEERNRKWLFYKGNL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022227"
FT   VAR_SEQ         2150
FT                   /note="Q -> QITGRDDPAKCGVERPYTTRVTSKGTAAVPVVSISSSAEV (in
FT                   isoform 4)"
FT                   /id="VSP_058822"
FT   CONFLICT        1886..1887
FT                   /note="Missing (in Ref. 1; ADK73961)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2150 AA;  245758 MW;  D7CDA1FE6476AB0E CRC64;
     MAGERTRRFT RSLLRPGQAA ELRHSAASAA AVAVSSRQQQ RQEKPRLLDP LDYETVIEEL
     EKTYRDDPLQ DLLFFPSDDF STATVSWDIR TLYSTVPEEA EHRAESLLVK EACKFYSSQW
     YVVNYKYEQY SGDIRQLPRA EHKPEKLPSH SFEVDHEDAD KDEDTTSHSS SKGGGGAGGT
     GVFKSGWLYK GNFNSTVNNT VTVRSFKKRY FQLTQLPDNS YIMNFYKDEK ISKEPKGCIF
     LDSCTGVVQN NRLRKYAFEL KMNDLTYFVL AAETESDMDE WIHTLNRILQ ISPEGPLQGR
     KSAELAELGL DPLDNCVTCE CTLEETDSSE NSLHPDFAKY LTETEDTVKT TRNMGRLNLF
     SLDPDIDTLK LQKRDSFENE LMIKPFEEKA AKRIMIICRA LNFNLQGCVT ENEYDPVTNI
     EPFFVSVALY DLRDNRKISA DFHVDLNHPA VRQMLSGTPP ALENGNIDTG TPRQSEEPHI
     KGLPEEWLKF PKQAVFSVSD PHSEIVLVAK VEKVLMGNIG SGAEPYIKNP DSNKFAQKIL
     KSNRQFCSKL GKYRMPFAWA VRSVFKDNQG NVDRDSRFSP LYRQESSKMS SEDLLKLVSD
     YRRADRISKM QSIPGSLDIA VDNIPLEHPN CVTSSFIPVK PFNVSAQSEP TVEVEEFIYD
     STKYCRPYRV YKNQIYVYPK HLKYDSQKCF NKARNITVCI EFKNSDDDGA KPMKCIYGKP
     GGPLFTSSAY TAVLHHSQNP DFSDEVKIEL PTQLHGKHHL LFSFYHITCD INAKANAKKK
     EALETSVGYA WLPLMKHDQI ASQEYNIPIA TTLPPNYLSI QDPTSAKHGG SDIKWVDGGK
     PLFKVSTFVV STVNTQDPHV NAFFRQCQKR EKDMSQSPTS SFVRACKNLL NVDKIHSIMS
     FLPIILNQLF KILVQNEEDE ITATVTRVLA DIVAKCHEEQ LDHSVQSYIK FVFKTKSYKE
     RTIHEELAKN LSDLLKSNDS TIVKHVLEHS WFFFAIILKS MAQHLIDTNK IQLPRAQRFP
     ESYQSELDNL VMGLCDHVIW KCKEAPEETK RANHSVARFL KRCFTFMDRG FVFKMVNNYI
     SMFSSGEFKT LCQYKFDFLQ EVCQHEHFIP LCLPIRSANI PDPLTPSESI RELHASDMPE
     YSVTNEFCRK HFLIGILLRE VGFALQEDQD IRHLALAVLK NLMAKHSFDD RYREPRKQAQ
     IASLYMPLYG MLLDNMPRIY LKDLYPFTVN TSNQGSRDDL STNGGFQTQT SMKHATSVDT
     SFSKDVLNSI AAFSSIAIST VNHADSRASL ASLDSNPSTT EKSSEKTDNC EKIPRPLSLI
     GSTLRFDKLD QAETRSLLMC FLHIMKTISD ETLIAYWQRA PSPEVSDFFS ILDVCLQNFR
     YLGKRNIIRK IAAAFKFVQS TQNNGTLKGS NPSCQTSGLL SQWMHTTSGH EGHKQHRSQT
     LPIIRGKNAL SNPKLLQMLD NSMNSNSNEI DIVHHVDTEA NIATEVCLTI LDLLSLFTQV
     HQRQLQQSDC QNSLMKRVFD TYMLFFQVNQ SASALKHVFA SLRLFVCKFP SAFFQGPADL
     CGSFCYEVLK CCNHRSRLTQ MEASALLYFF MRKNFEFNKQ KSIVRSHLQL IKAVSQLIAD
     AGIGGSRFQH SLAITNNFAN GDKQMKNSNF PAEVKDLTKR IRTVLMATAQ MKEHEKDPEM
     LVDLQYSLAN SYASTPELRR TWLESMAKIH ARNGDLSEAA MCYIHIAALI AEYLKRKGYW
     KMEKICTPPL LPEDTQPCDS NLLLTTPGGG SMFSMGWPAF LSITPNIKEE GAMKEDSGMQ
     DTPYNENILV EQLYMCVEFL WKSERYELIA DVNKPIIAVF EKQRDFKKLS DLYYDIHRSY
     LKVAEVVNSE KRLFGRYYRV AFYGQAVGFF EEEEGKEYIY KEPKLTGLSE ISQRLLKLYA
     DKFGADNVKI IQDSNKVNPK DLDPKYAYIQ VTYVTPFFEE KEIEDRKTDF EMHHNINRFV
     FETPFTLSGK KHGGVAEQCK RRTVLTTSHL FPYVKKRIQV ISQSSTELNP IEVAIDEMSR
     KVSELNQLCT TEEVDMIRLQ LKLQGSVSVK VNAGPMAYAR AFLEETNAKK YPDNQVKLLK
     EIFRQFADAC GQALDVNERL IKEDQLEYQE ELRSHYKDML SELSAIMNEQ
 
 
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