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BAKOR_MOUSE
ID   BAKOR_MOUSE             Reviewed;         492 AA.
AC   Q8CDJ3; Q69ZY1; Q6PFY6; Q8C6N0; Q8R3M3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Beclin 1-associated autophagy-related key regulator {ECO:0000250|UniProtKB:Q6ZNE5};
DE            Short=Barkor {ECO:0000250|UniProtKB:Q6ZNE5};
DE   AltName: Full=Autophagy-related protein 14-like protein {ECO:0000303|PubMed:19270696};
DE            Short=Atg14L {ECO:0000303|PubMed:19270696};
GN   Name=Atg14 {ECO:0000312|MGI:MGI:1261775};
GN   Synonyms=Atg14L {ECO:0000303|PubMed:19270696}, D14Ertd436e, Kiaa0831;
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].
RC   STRAIN=C57BL/6J; TISSUE=Oviduct, and Testis;
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 MRNA].
RC   STRAIN=C57BL/6J, and FVB/N;
RC   TISSUE=Embryonic brain, Heart, and 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-492.
RC   TISSUE=Spleen;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=18843052; DOI=10.1091/mbc.e08-01-0080;
RA   Itakura E., Kishi C., Inoue K., Mizushima N.;
RT   "Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with
RT   mammalian Atg14 and UVRAG.";
RL   Mol. Biol. Cell 19:5360-5372(2008).
RN   [5]
RP   FUNCTION.
RX   PubMed=19270696; DOI=10.1038/ncb1846;
RA   Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N.,
RA   Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T.,
RA   Yoshimori T.;
RT   "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate
RT   autophagy at different stages.";
RL   Nat. Cell Biol. 11:385-396(2009).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1 AND PIK3C3.
RX   PubMed=19270693; DOI=10.1038/ncb1854;
RA   Zhong Y., Wang Q.J., Li X., Yan Y., Backer J.M., Chait B.T., Heintz N.,
RA   Yue Z.;
RT   "Distinct regulation of autophagic activity by Atg14L and Rubicon
RT   associated with Beclin 1-phosphatidylinositol-3-kinase complex.";
RL   Nat. Cell Biol. 11:468-476(2009).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20639694; DOI=10.4161/auto.6.6.12709;
RA   Itakura E., Mizushima N.;
RT   "Characterization of autophagosome formation site by a hierarchical
RT   analysis of mammalian Atg proteins.";
RL   Autophagy 6:764-776(2010).
RN   [8]
RP   INTERACTION WITH PIK3CB.
RX   PubMed=21059846; DOI=10.1083/jcb.201006056;
RA   Dou Z., Chattopadhyay M., Pan J.-A., Guerriero J.L., Jiang Y.-P.,
RA   Ballou L.M., Yue Z., Lin R.Z., Zong W.-X.;
RT   "The class IA phosphatidylinositol 3-kinase p110-beta subunit is a positive
RT   regulator of autophagy.";
RL   J. Cell Biol. 191:827-843(2010).
RN   [9]
RP   DOMAIN, AND SUBCELLULAR LOCATION.
RX   PubMed=21518905; DOI=10.1073/pnas.1016472108;
RA   Fan W., Nassiri A., Zhong Q.;
RT   "Autophagosome targeting and membrane curvature sensing by
RT   Barkor/Atg14(L).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:7769-7774(2011).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22863730; DOI=10.4161/auto.21459;
RA   Aguilera M.O., Beron W., Colombo M.I.;
RT   "The actin cytoskeleton participates in the early events of autophagosome
RT   formation upon starvation induced autophagy.";
RL   Autophagy 8:1590-1603(2012).
RN   [11]
RP   IDENTIFICATION IN THE PI3-KINASE COMPLEX I.
RX   PubMed=22745922; DOI=10.1016/j.celrep.2012.03.014;
RA   Yamada E., Bastie C.C., Koga H., Wang Y., Cuervo A.M., Pessin J.E.;
RT   "Mouse skeletal muscle fiber-type-specific macroautophagy and muscle
RT   wasting are regulated by a Fyn/STAT3/Vps34 signaling pathway.";
RL   Cell Rep. 1:557-569(2012).
RN   [12]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=22992773; DOI=10.1074/jbc.m112.412569;
RA   Xiong X., Tao R., DePinho R.A., Dong X.C.;
RT   "The autophagy-related gene 14 (Atg14) is regulated by forkhead box O
RT   transcription factors and circadian rhythms and plays a critical role in
RT   hepatic autophagy and lipid metabolism.";
RL   J. Biol. Chem. 287:39107-39114(2012).
RN   [13]
RP   FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH PIK3C3; PIK3R4 AND BECN1.
RX   PubMed=23332761; DOI=10.1016/j.cell.2012.12.016;
RA   Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R.,
RA   Zhong Q., Guan K.L.;
RT   "Differential regulation of distinct Vps34 complexes by AMPK in nutrient
RT   stress and autophagy.";
RL   Cell 152:290-303(2013).
RN   [14]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24089209; DOI=10.1038/nature12639;
RA   Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA   Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT   "Functional interaction between autophagy and ciliogenesis.";
RL   Nature 502:194-200(2013).
RN   [15]
RP   INTERACTION WITH NRBF2.
RX   PubMed=24849286; DOI=10.1038/ncomms4920;
RA   Lu J., He L., Behrends C., Araki M., Araki K., Jun Wang Q., Catanzaro J.M.,
RA   Friedman S.L., Zong W.X., Fiel M.I., Li M., Yue Z.;
RT   "NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-
RT   linked phosphatidylinositol-3 kinase III activity.";
RL   Nat. Commun. 5:3920-3920(2014).
CC   -!- FUNCTION: Required for both basal and inducible autophagy
CC       (PubMed:19270696, PubMed:19270693). Determines the localization of the
CC       autophagy-specific PI3-kinase complex PI3KC3-C1 (By similarity). Plays
CC       a role in autophagosome formation and MAP1LC3/LC3 conjugation to
CC       phosphatidylethanolamine (PubMed:19270696, PubMed:19270693). Promotes
CC       BECN1 translocation from the trans-Golgi network to autophagosomes (By
CC       similarity). Enhances PIK3C3 activity in a BECN1-dependent manner.
CC       Essential for the autophagy-dependent phosphorylation of BECN1 (By
CC       similarity). Stimulates the phosphorylation of BECN1, but suppresses
CC       the phosphorylation of PIK3C3 by AMPK (PubMed:23332761). Binds to
CC       STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for
CC       VAMP8 interaction to promote autophagosome-endolysosome fusion (By
CC       similarity). Modulates the hepatic lipid metabolism (PubMed:22992773).
CC       {ECO:0000250|UniProtKB:Q6ZNE5, ECO:0000269|PubMed:19270693,
CC       ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:22992773,
CC       ECO:0000269|PubMed:23332761}.
CC   -!- SUBUNIT: Forms homooligomers; homo-oligomerization is essential for the
CC       roles in membrane tethering and enhancement of SNARE-mediated fusion
CC       (By similarity). Component of the PI3K (PI3KC3/PI3K-III/class III
CC       phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core
CC       composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4
CC       and BECN1 is associated with ATG14 (PubMed:19270693, PubMed:22745922,
CC       PubMed:23332761). PI3KC3-C1 displays a V-shaped architecture with
CC       PIK3R4 serving as a bridge between PIK3C3 and the ATG14:BECN1
CC       subcomplex (By similarity). PI3KC3-C1 can associate with further
CC       regulatory subunits (PubMed:24849286). Interacts with PIK3CB
CC       (PubMed:21059846). Interacts (via coiled-coil domain) with BECN2 (via
CC       coiled-coil domain); this interaction is tighter than BECN2 self-
CC       association (By similarity). Interacts with the STX17-SNAP29 binary t-
CC       SNARE complex (By similarity). Interacts with NRBF2 (PubMed:24849286)
CC       Interacts with PIK3C3 and BECN1; this interaction is increased in the
CC       absence of TMEM39A (By similarity). Interacts with STEEP1; the
CC       interaction is required for trafficking of STING1 from the endoplasmic
CC       reticulum (By similarity). {ECO:0000250|UniProtKB:Q6ZNE5,
CC       ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:21059846,
CC       ECO:0000269|PubMed:22745922, ECO:0000269|PubMed:23332761,
CC       ECO:0000269|PubMed:24849286}.
CC   -!- INTERACTION:
CC       Q8CDJ3; P23242: Gja1; NbExp=2; IntAct=EBI-3506699, EBI-298630;
CC       Q8CDJ3; Q8VCQ3: Nrbf2; NbExp=7; IntAct=EBI-3506699, EBI-2365563;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639694}.
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:20639694};
CC       Peripheral membrane protein {ECO:0000305}. Preautophagosomal structure
CC       membrane {ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:20639694,
CC       ECO:0000269|PubMed:22863730}; Peripheral membrane protein
CC       {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000250|UniProtKB:Q6ZNE5}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Cytosolic under nutrient-rich conditions
CC       (PubMed:20639694). Following autophagy stimuli, such as starvation or
CC       rapamycin induction, predominantly detected in cytoplasmic foci,
CC       identified as isolation membranes and autophagosomes (PubMed:20639694).
CC       Accumulates on highly curved PtdIns(3)P enriched autophagic membrane
CC       via its BATS domain to sense and maintain membrane curvature
CC       (PubMed:21518905). Localizes also to discrete punctae along the ciliary
CC       axoneme and to the base of the ciliary axoneme (PubMed:24089209).
CC       {ECO:0000269|PubMed:20639694, ECO:0000269|PubMed:21518905,
CC       ECO:0000269|PubMed:24089209}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18843052}.
CC   -!- INDUCTION: Expression is controlled by forkhead box O FoxO1
CC       transcription factor and circadian rhythms.
CC       {ECO:0000269|PubMed:22992773}.
CC   -!- DOMAIN: The coiled-coil domain is required for BECN1- and PIK3C3-
CC       binding and for autophagy. {ECO:0000250|UniProtKB:Q6ZNE5}.
CC   -!- DOMAIN: The final 80 residues in the C-terminus define a minimum
CC       required region for autophagosome binding called BATS.
CC       {ECO:0000269|PubMed:21518905}.
CC   -!- DOMAIN: The N-terminal cysteine repeats are required for proper
CC       localization to the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:Q6ZNE5}.
CC   -!- SIMILARITY: Belongs to the ATG14 family. {ECO:0000305}.
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DR   EMBL; AK029967; BAC26705.1; -; mRNA.
DR   EMBL; AK054196; BAC35689.1; -; mRNA.
DR   EMBL; BC025038; AAH25038.1; -; mRNA.
DR   EMBL; BC057360; AAH57360.1; -; mRNA.
DR   EMBL; BC090995; AAH90995.1; -; mRNA.
DR   EMBL; AK173037; BAD32315.1; -; mRNA.
DR   CCDS; CCDS26989.1; -.
DR   RefSeq; NP_766187.1; NM_172599.4.
DR   AlphaFoldDB; Q8CDJ3; -.
DR   SMR; Q8CDJ3; -.
DR   BioGRID; 425286; 5.
DR   ComplexPortal; CPX-75; Phosphatidylinositol 3-kinase complex, class III, ATG14 variant.
DR   DIP; DIP-60849N; -.
DR   IntAct; Q8CDJ3; 13.
DR   MINT; Q8CDJ3; -.
DR   STRING; 10090.ENSMUSP00000039047; -.
DR   iPTMnet; Q8CDJ3; -.
DR   PhosphoSitePlus; Q8CDJ3; -.
DR   EPD; Q8CDJ3; -.
DR   MaxQB; Q8CDJ3; -.
DR   PaxDb; Q8CDJ3; -.
DR   PeptideAtlas; Q8CDJ3; -.
DR   PRIDE; Q8CDJ3; -.
DR   ProteomicsDB; 273597; -.
DR   Antibodypedia; 24031; 224 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000042988; ENSMUSP00000039047; ENSMUSG00000037526.
DR   Ensembl; ENSMUST00000226299; ENSMUSP00000153718; ENSMUSG00000037526.
DR   GeneID; 100504663; -.
DR   KEGG; mmu:100504663; -.
DR   UCSC; uc007tik.2; mouse.
DR   CTD; 22863; -.
DR   MGI; MGI:1261775; Atg14.
DR   VEuPathDB; HostDB:ENSMUSG00000037526; -.
DR   eggNOG; KOG4398; Eukaryota.
DR   GeneTree; ENSGT00390000011854; -.
DR   HOGENOM; CLU_046719_1_0_1; -.
DR   InParanoid; Q8CDJ3; -.
DR   OMA; PWITLPN; -.
DR   OrthoDB; 1332122at2759; -.
DR   PhylomeDB; Q8CDJ3; -.
DR   TreeFam; TF323392; -.
DR   Reactome; R-MMU-1632852; Macroautophagy.
DR   BioGRID-ORCS; 100504663; 22 hits in 72 CRISPR screens.
DR   PRO; PR:Q8CDJ3; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q8CDJ3; protein.
DR   Bgee; ENSMUSG00000037526; Expressed in morula and 248 other tissues.
DR   ExpressionAtlas; Q8CDJ3; baseline and differential.
DR   Genevisible; Q8CDJ3; MM.
DR   GO; GO:0005776; C:autophagosome; ISO:MGI.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097629; C:extrinsic component of omegasome membrane; ISO:MGI.
DR   GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; ISO:MGI.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR   GO; GO:0034045; C:phagophore assembly site membrane; ISO:MGI.
DR   GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IDA:UniProtKB.
DR   GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR   GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR   GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR   GO; GO:0016240; P:autophagosome membrane docking; ISO:MGI.
DR   GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR   GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR   GO; GO:0016236; P:macroautophagy; ISO:MGI.
DR   GO; GO:0000423; P:mitophagy; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR   GO; GO:0006622; P:protein targeting to lysosome; IC:ComplexPortal.
DR   GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:MGI.
DR   GO; GO:0098780; P:response to mitochondrial depolarisation; ISO:MGI.
DR   InterPro; IPR018791; UV_resistance/autophagy_Atg14.
DR   Pfam; PF10186; ATG14; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Beclin 1-associated autophagy-related key regulator"
FT                   /id="PRO_0000050775"
FT   REGION          410..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..492
FT                   /note="BATS"
FT   REGION          451..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          70..180
FT                   /evidence="ECO:0000255"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZNE5"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZNE5"
FT   MOD_RES         429
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZNE5"
SQ   SEQUENCE   492 AA;  55388 MW;  A221B3C03C8E2F9A CRC64;
     MASPSGKGSW TPEAPGFGPR ALARDLVDSV DDAEGLYVAV ERCPLCNTTR RRLTCAKCVQ
     SGDFVYFDGR DRERFIDKKE RLSQLKNKQE EFQKEVLKAM EGKRLTDQLR WKIMSCKMRI
     EQLKQTICKG NEEMKKNSEG LLKNKEKNQK LYSRAQRHQE KKEKIQRHNR KLGDLVEKKT
     IDLKSHYERL ARLRRSHILE LTSIIFPIDE VKTSGRDPAD VSSETDSAMT SSMVSKLAEA
     RRTTYLSGRW VCDDHNGDTS ISITGPWISL PNNGDYSAYY NWVEEKKTTQ GPDMEHNNPA
     YTISAALGYA TQLVNIVSHI LDINLPKKLC NSEFCGENLS KQKLTRAVRK LNANILYLCS
     SQHVNLDQLQ PLHTLRNLMH LVSPRSEHLG RSGPFEVRAD LEESMEFVDP GVAGESDASG
     DERVSDEETD LGTDWENLPS PRFCDIPSQP VEVSQSQSTQ VSPPIASSSA GGMISSAAAS
     VTSWFKAYTG HR
 
 
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