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NBEA_DROME
ID   NBEA_DROME              Reviewed;        3466 AA.
AC   Q9W4E2; O16024; Q8IRR9; Q961G8; Q9GP69; Q9GP70;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 4.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Neurobeachin;
DE   AltName: Full=A-kinase anchor protein 550;
DE            Short=AKAP 550;
DE   AltName: Full=Protein rugose;
DE   AltName: Full=dAKAP550;
GN   Name=rg; Synonyms=Akap550; ORFNames=CG44835;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000305}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537572};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 197-3466 (ISOFORM N), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Head {ECO:0000269|PubMed:11102458};
RX   PubMed=11102458; DOI=10.1523/jneurosci.20-23-08551.2000;
RA   Wang X., Herberg F.W., Laue M.M., Wullner C., Hu B., Petrasch-Parwez E.,
RA   Kilimann M.W.;
RT   "Neurobeachin: a protein kinase A-anchoring, beige/Chediak-Higashi protein
RT   homolog implicated in neuronal membrane traffic.";
RL   J. Neurosci. 20:8551-8565(2000).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 197-2271 (ISOFORM N), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Canton-S {ECO:0000269|PubMed:9334242};
RC   TISSUE=Embryo {ECO:0000269|PubMed:9334242};
RX   PubMed=9334242; DOI=10.1074/jbc.272.42.26611;
RA   Han J.-D., Baker N.E., Rubin C.S.;
RT   "Molecular characterization of a novel A kinase anchor protein from
RT   Drosophila melanogaster.";
RL   J. Biol. Chem. 272:26611-26619(1997).
RN   [5] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2478-3466 (ISOFORMS N/R).
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Head {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6] {ECO:0000305}
RP   FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=12072466; DOI=10.1093/genetics/161.2.693;
RA   Shamloula H.K., Mbogho M.P., Pimentel A.C., Chrzanowska-Lightowlers Z.M.,
RA   Hyatt V., Okano H., Venkatesh T.R.;
RT   "rugose (rg), a Drosophila A kinase anchor protein, is required for retinal
RT   pattern formation and interacts genetically with multiple signaling
RT   pathways.";
RL   Genetics 161:693-710(2002).
RN   [7] {ECO:0000305}
RP   INTERACTION WITH NOTCH-MEDIATED SIGNALING PATHWAY.
RX   PubMed=12124948; DOI=10.1002/gene.10102;
RA   Schreiber S.L., Preiss A., Nagel A.C., Wech I., Maier D.;
RT   "Genetic screen for modifiers of the rough eye phenotype resulting from
RT   overexpression of the Notch antagonist hairless in Drosophila.";
RL   Genesis 33:141-152(2002).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23100440; DOI=10.1523/jneurosci.6424-11.2012;
RA   Volders K., Scholz S., Slabbaert J.R., Nagel A.C., Verstreken P.,
RA   Creemers J.W., Callaerts P., Schwarzel M.;
RT   "Drosophila rugose is a functional homolog of mammalian Neurobeachin and
RT   affects synaptic architecture, brain morphology, and associative
RT   learning.";
RL   J. Neurosci. 32:15193-15204(2012).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23790035; DOI=10.1111/gbb.12056;
RA   Zhao J., Lu Y., Zhao X., Yao X., Shuai Y., Huang C., Wang L., Jeong S.H.,
RA   Zhong Y.;
RT   "Dissociation of rugose-dependent short-term memory component from memory
RT   consolidation in Drosophila.";
RL   Genes Brain Behav. 12:626-632(2013).
CC   -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC       anchors/targets them to the membrane. May anchor the kinase to
CC       cytoskeletal and/or organelle-associated proteins. Required for correct
CC       retinal pattern formation and may function in cell fate determination
CC       through its interactions with the EGFR and Notch signaling pathways.
CC       Required for associative odor learning and short-term memory. Involved
CC       in development of the neuromuscular junction and the mushroom body.
CC       {ECO:0000269|PubMed:11102458, ECO:0000269|PubMed:12072466,
CC       ECO:0000269|PubMed:23100440, ECO:0000269|PubMed:23790035,
CC       ECO:0000269|PubMed:9334242}.
CC   -!- SUBUNIT: Interacts with RII subunit of PKA and components of the EGFR-
CC       mediated and Notch-mediated signaling pathways.
CC       {ECO:0000269|PubMed:11102458, ECO:0000269|PubMed:12072466,
CC       ECO:0000269|PubMed:12124948, ECO:0000269|PubMed:9334242}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC       Perikaryon. Note=Found in the cortical region of perikarya with no
CC       expression in neuropil regions. Located at or near the Golgi network in
CC       perikarya of the dorsal medial cluster neurons.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=N {ECO:0000312|FlyBase:FBgn0266098};
CC         IsoId=Q9W4E2-5; Sequence=Displayed;
CC       Name=R {ECO:0000312|FlyBase:FBgn0266098};
CC         IsoId=Q9W4E2-6; Sequence=VSP_058161, VSP_058162, VSP_058163,
CC                                  VSP_058164;
CC   -!- TISSUE SPECIFICITY: In early embryos, ubiquitous expression with
CC       elevated levels in ventral furrow and flanking mesectodermal cells,
CC       neuroblasts and mesoderm. Late embryos show reduced expression in
CC       epidermis and skeletal muscle and elevated in nervous system, gut
CC       endothelium, tracheal system and salivary gland. Larvae show expression
CC       in imaginal disks and many neural cells. Developing eye imaginal disk
CC       shows expression throughout the disk and in the region of the
CC       morphogenetic furrow. Ubiquitous expression in adults with higher
CC       levels in head region. Expressed in larval neurons but not in larval
CC       glia. {ECO:0000269|PubMed:12072466, ECO:0000269|PubMed:23100440,
CC       ECO:0000269|PubMed:9334242}.
CC   -!- DEVELOPMENTAL STAGE: All stages of development.
CC       {ECO:0000269|PubMed:9334242}.
CC   -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC       could participate in protein-protein interactions with a complementary
CC       surface on the R-subunit dimer. {ECO:0000303|PubMed:11102458}.
CC   -!- DISRUPTION PHENOTYPE: Mutants are viable and fertile but display a
CC       rough eye surface phenotype, impaired short-term memory, aberrant
CC       associative odor learning, aberrant neuromuscular junction morphology
CC       with increased numbers of synaptic boutons, and defective axonal
CC       morphology of the Kenyon cells, the neurons of the mushroom body.
CC       {ECO:0000269|PubMed:23100440, ECO:0000269|PubMed:23790035}.
CC   -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB83959.1; Type=Miscellaneous discrepancy; Note=Intron retention. In addition to the intron retained at the N-terminus, there are other discrepancies towards the C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAK93020.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAC18799.1; Type=Miscellaneous discrepancy; Note=Intron retention. In addition, there are retained or missing exons which cannot be reconciled with any described isoform.; Evidence={ECO:0000305};
CC       Sequence=CAC18800.1; Type=Miscellaneous discrepancy; Note=Intron retention. In addition, there are retained or missing exons which cannot be reconciled with any described isoform.; Evidence={ECO:0000305};
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DR   EMBL; AE014298; AAF46011.4; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09135.1; -; Genomic_DNA.
DR   EMBL; Y18278; CAC18799.1; ALT_SEQ; mRNA.
DR   EMBL; Y18278; CAC18800.1; ALT_SEQ; mRNA.
DR   EMBL; AF003622; AAB83959.1; ALT_SEQ; mRNA.
DR   EMBL; AY051596; AAK93020.1; ALT_INIT; mRNA.
DR   PIR; T03094; T03094.
DR   RefSeq; NP_001138158.2; NM_001144686.2. [Q9W4E2-5]
DR   RefSeq; NP_726978.2; NM_167028.3. [Q9W4E2-6]
DR   SMR; Q9W4E2; -.
DR   BioGRID; 69112; 13.
DR   DIP; DIP-17945N; -.
DR   IntAct; Q9W4E2; 2.
DR   STRING; 7227.FBpp0288527; -.
DR   PaxDb; Q9W4E2; -.
DR   EnsemblMetazoa; FBtr0344649; FBpp0310996; FBgn0266098. [Q9W4E2-5]
DR   EnsemblMetazoa; FBtr0344668; FBpp0311009; FBgn0266098. [Q9W4E2-6]
DR   GeneID; 44531; -.
DR   KEGG; dme:Dmel_CG44835; -.
DR   CTD; 44531; -.
DR   FlyBase; FBgn0266098; rg.
DR   VEuPathDB; VectorBase:FBgn0266098; -.
DR   eggNOG; KOG1787; Eukaryota.
DR   InParanoid; Q9W4E2; -.
DR   BioGRID-ORCS; 44531; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; rg; fly.
DR   GenomeRNAi; 44531; -.
DR   PRO; PR:Q9W4E2; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0266098; Expressed in brain and 25 other tissues.
DR   ExpressionAtlas; Q9W4E2; baseline and differential.
DR   Genevisible; Q9W4E2; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:UniProtKB.
DR   GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR   GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR   CDD; cd06071; Beach; 1.
DR   CDD; cd01201; PH_BEACH; 1.
DR   Gene3D; 1.10.1540.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000409; BEACH_dom.
DR   InterPro; IPR036372; BEACH_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR010508; NBEA-like_DUF1088.
DR   InterPro; IPR031570; NBEA/BDCP_DUF4704.
DR   InterPro; IPR023362; PH-BEACH_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF06469; DUF1088; 1.
DR   Pfam; PF15787; DUF4704; 1.
DR   Pfam; PF14844; PH_BEACH; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM01026; Beach; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF81837; SSF81837; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS51783; PH_BEACH; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Membrane; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..3466
FT                   /note="Neurobeachin"
FT                   /id="PRO_0000051093"
FT   REPEAT          1846..1888
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2666..2774
FT                   /note="BEACH-type PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT   DOMAIN          2793..3082
FT                   /note="BEACH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT   REPEAT          3241..3284
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3298..3338
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3380..3419
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          3422..3461
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REGION          523..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1363..1382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1393..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1601..1695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1794..1848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2105..2130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2198..2257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2284..2365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1393..1441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1558..1574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1605..1691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1716..1739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1747..1767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1794..1840
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2218..2236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2240..2254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2297..2316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         2..53
FT                   /note="ADIMRPPYSEIKRPDEIVRMTTADNLKFAVLIGLIEVGQVTNREVVNTVLHL
FT                   -> DSLERLMRAAPLPRMLTSGVVATAAAAASAAAGKGMVSVGGGATAIAAGGGQQRAL
FT                   VHASLAAATVGRKGRHLTGTFCLTGDTMEGIIQCLVFLKAFS (in isoform R)"
FT                   /id="VSP_058161"
FT   VAR_SEQ         388..594
FT                   /note="Missing (in isoform R)"
FT                   /id="VSP_058162"
FT   VAR_SEQ         759..768
FT                   /note="Missing (in isoform R)"
FT                   /id="VSP_058163"
FT   VAR_SEQ         2159..2214
FT                   /note="Missing (in isoform R)"
FT                   /id="VSP_058164"
FT   CONFLICT        218
FT                   /note="F -> C (in Ref. 3; CAC18799/CAC18800 and 4;
FT                   AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="C -> S (in Ref. 3; CAC18799/CAC18800 and 4;
FT                   AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        411
FT                   /note="T -> A (in Ref. 3; CAC18799 and 4; AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415
FT                   /note="T -> S (in Ref. 3; CAC18799 and 4; AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="H -> D (in Ref. 3; CAC18799 and 4; AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590
FT                   /note="N -> D (in Ref. 3; CAC18799 and 4; AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1702
FT                   /note="N -> T (in Ref. 3; CAC18799/CAC18800 and 4;
FT                   AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2230..2239
FT                   /note="ENEVPEVESS -> GKTKCPRWSHP (in Ref. 3; CAC18799/
FT                   CAC18800 and 4; AAB83959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2576
FT                   /note="V -> G (in Ref. 3; CAC18799/CAC18800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3466 AA;  384513 MW;  152AEB5152C8F37C CRC64;
     MADIMRPPYS EIKRPDEIVR MTTADNLKFA VLIGLIEVGQ VTNREVVNTV LHLLVGGEFD
     MELNFVIQDA QNIKHMLELL DHCPPNLQAE IWSVFIAILR KSVRNLQACT DVGLIEHVLV
     RLQRSETVVA DLLIEMLGVL ASYSITVKEL KLLFGTMKAT NGKWPRHSAK LLNVLRQMPH
     RNGPDVFFSF PGRKGSAMVL PPLAKWPYEN GFTFTTWFRL DPINSVNIER EKPYLYCFKT
     SKGVGYTAHF VGNCLVLTSM KVKGKGFQHC VKYEFQPRKW YMIAIVYIYN RWTKSEIKCL
     VNGQLASSTE MAWFVSTNDP FDKCYIGATP ELDEERVFCG QMSAIYLFSE ALTTQQICAM
     HRLGPGYKSQ FRFDNECYLN LPDNHKRVSH FQLLPATLGA SALSGGSGSG TGSGTGNDAS
     AAAAAAVAAG QQQQLQLQFQ ILAAEQEARA IDWSDEKLDL NAAFVKIRAV LTARNAVTLA
     GSSSTGTTAV ATAAAAAAAA GAGAGTTAAA TSAAAAAAAT QNENDAAVGQ QQHATHHHAT
     AATGSADDPL GHLPTGNASS SSSSFEQLRR MSSVSSLNSM VGSADTEEVN QLKAVLYDGK
     LSNAIVFMYN PVATDGQLCL QSSPKGNVSY FVHTPHALML QDVKAVVTHS IHCTLNSIGG
     IQVLFPLFSQ LDMAHEGLGD IKRDPTLCSK LLGFICELVE TSQTVQQHMI QNRGFLVISF
     MLQRSSREHL TLEVLGSFLN LTKYLVTCLS ANSDLLLKQL FCFSFLTWQL LDHVLFNPAL
     WIYTPANVQA RLYSYLATEF LSDTQIYSNV RRVSTVLQTV HTLKYYYWVV NPRAKSGIIP
     KGLDGPRPAQ KDILAIRAYI LLFLKQLIMI GNGVKEDELQ SILNYLTTMH EDENLHDVLQ
     MLISLMSEHP SSMVPAFDVK HGVRSIFKLL AAESQLIRLQ ALKLLGFFLS RSTHKRKYDV
     MSPHNLYTLL AERLLLYEES LSLPTYNVLY EIMTEHISQQ ILYTRHPEPE SHYRLENPMI
     LKVVATLIRQ SKQTESLIDV KKLFLQDMTL LCNSNRENRR TVLQMSVWQE WLIAMAYIHP
     KSSEEQKISD MVYSLFRMLL HHAIKHEYGG WRVWVDTLAI VHSKVSYEEF KLQFAQMYEH
     YERQRTDNIT DPALRQARPI STISGWEREE LHQQQNGGSA AAVATNQTAA VKGSVSIASL
     EDVPPVVEEE VEELELEEVE IQEGPITEET EQKSVIANIS DVYNEQLKTD ATCNGNLEDV
     KEEEPVQQQI GDLEKQPEPS TPLGALRETL QLGDDMDVEE LELATAKDAL NAEQHVSRVL
     QASEAALNDC KMAVDDVLQE SSSVLKDEEI ELAVNEVVQG VLNNEKKTQS QDNKDNKEQP
     GEQDVNVSLL NSKNLLNNNN NNNNNSPSPT PTTATATAET EAETEVNANE IVSSTEAPKA
     ETETSVAPEV ETPETAKPSP IVPSPVLATN QKTEDAANKL NNNEKLAEIS ASPEPPIVVE
     TPEADLLQLS DSETKPNKET EAEDSVALAV RDIVEQLIDK VIDATEAESA SETKTETNNN
     EIPKKEKQTS EEPEDVETAE TLAAAAKEIV QEVVEAALVM VQEESTQEKP EKGANSEEEK
     NEIGKEEILL QLEEKPASTE VQETKIEGDL KKPEDPKGHS SVEPKTPNLE EPKPQETEQQ
     KSQEVAEELP QKPEEQVVAI VNQVLDTLVD DTVKAVAAEQ TTQTSPAPEE QSPQILAMES
     PATSVRVKPT EVDSTTQTTP KNEAGSSLLV EQVQQVLQED DAQQSAGMTI EDEDYSNQQA
     AAAVENANSS QLDANHYGPG NPESKQQQQR SKSGSTRPMF SPGPTRPPFR IPEFKWSYIH
     QRLLSDVLFS LETDIQVWRS HSTKSVLDFV NSSENAIFVV NTVHLISQLA DNLIIACGGL
     LPLLASATSP NSELDVLEPT QGMPLEVAVS FLQRLVNMAD VLIFATSLNF GELEAEKNMS
     SGGILRQCLR LVCTCAVRNC LECKERTRYN VGALARDVPG AAHLQALIRG AQASPKNIVE
     SITGQLSPVK DPEKLLQDMD VNRLRAVIYR DVEETKQAQF LSLAIVYFIS VLMVSKYRDI
     LEPPAEPQIQ RQSPVLQRTA GGGGRQIQDS DYEIIVVDEN NPSVLADNDS HSSGPPSIKA
     NQTTTIATTT TTTATTHINN NNTKTTTSNA PTATIKIQQQ PLSPPKPLVP QKLPKSVDSD
     VGSLNMNSTE NEVPEVESSS EILIDDHKPS HSNDESWTDV NLNEDAAVQA ASAGIVVGLV
     DNRGNVISDK HDPSHHNQQQ QQQAGIIGQQ QQHGSLGHSE RGDKPDSEIS VVRVPDGYGG
     AGSGGGVNSG QGQGVPSNQR PRPEELPMKA PALVAQLPLT TPSREASLTQ KLEIALGPVC
     PLLREIMVDF APFLSKTLVG SHGQELLMEG KGLTTFKNSH SVVELVMLLC SQEWQNSLQK
     HAGLAFIELI NEGRLLSHAM KDHIVRVANE AEFILNRMRA DDVLKHADFE SQCAQTLLER
     REEERMCDHL ITAARRRDNV IASRLLEKVR NIMCNRHGAW GDSSSTSSGG AIVGAVQKSP
     YWKLDAWEDD ARRRKRMVQN PRGSSHPQAT LKAALENGGP EDAILQTRDE FHTQIAVSRT
     HPSGQHNGEL LDDAELLIED RELDLDLTGP VNISTKARLI APGLVAPGTV SITSTEMFFE
     VDEEHPEFQK IDGEVLKYCD HLHGKWYFSE VRAIFSRRYL LQNVALEIFL ASRTSILFAF
     PDQHTVKKVI KALPRVGVGI KYGIPQTRRA SMMSPRQLMR NSNMTQKWQR REISNFEYLM
     FLNTIAGRTY NDLNQYPIFP WVLTNYESKD LDLSLPSNYR DLSKPIGALN PSRRAYFEER
     YESWDSDTIP PFHYGTHYST AAFTLNWLVR VEPFTTMFLA LQGGKFDYPD RLFSSVSLSW
     KNCQRDTSDV KELIPEWYFL PEMFYNSSGY RLGHREDGAL VDDIELPPWA KSPEEFVRIN
     RMALESEFVS CQLHQWIDLI FGYKQRGPEA IRATNVFYYL TYEGSVDLDG VLDPVMREAV
     ENQIRNFGQT PSQLLMEPHP PRSSAMHLSP MMFSAMPEDL CQMLKFYQNS PVIHISANTY
     PQLSLPSVVT VTAGHQFAVN RWNCNYTASV QSPSYAESPQ SPGSNQPLTI DPVLAVHGTN
     NNSNAASRRH LGDNFSQMLK IRSNCFVTTV DSRFLIACGF WDNSFRVFAT ETAKIVQIVF
     GHFGVVTCMA RSECNITSDC YIASGSADCT VLLWHWNART QSIVGEGDVP TPRATLTGHE
     QAVTSVVISA ELGLVVSGSS NGPVLIHTTF GDLLRSLDPP AEFHSPELIT MSREGFIVIN
     YDKGNVAAYT INGKKLRHET HNDNLQCMLL SRDGEYLMTA GDRGIVEVWR TFNLAPLYAF
     PACNAGIRSL ALTHDQKYLL AGLSTGSIIV FHIDFNRWHH EYQQRY
 
 
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