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HTH_DROME
ID   HTH_DROME               Reviewed;         487 AA.
AC   O46339; O17427; Q058V1; Q4AB34; Q59DX7; Q6NR42; Q7KQ21; Q8INL5; Q8INL6;
AC   Q9VGY9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=Homeobox protein homothorax;
DE   AltName: Full=Homeobox protein dorsotonals;
GN   Name=hth {ECO:0000312|FlyBase:FBgn0001235};
GN   Synonyms=dtl {ECO:0000312|EMBL:AAB97169.1}; ORFNames=CG17117;
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] {ECO:0000305, ECO:0000312|EMBL:AAC47759.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H), FUNCTION, INTERACTION WITH EXD,
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Antenna {ECO:0000312|EMBL:AAC47759.1};
RX   PubMed=9346235; DOI=10.1016/s0092-8674(00)80400-6;
RA   Rieckhof G.E., Casares F., Ryoo H.D., Abu-Shaar M., Mann R.S.;
RT   "Nuclear translocation of extradenticle requires homothorax, which encodes
RT   an extradenticle-related homeodomain protein.";
RL   Cell 91:171-183(1997).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAB97169.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, INTERACTION WITH EXD, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9463350; DOI=10.1242/dev.125.6.1037;
RA   Kurant E., Pai C.-Y., Sharf R., Halachmi N., Sun Y.H., Salzberg A.;
RT   "Dorsotonals/homothorax, the Drosophila homologue of meis1, interacts with
RT   extradenticle in patterning of the embryonic PNS.";
RL   Development 125:1037-1048(1998).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAB88514.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), FUNCTION, INTERACTION WITH
RP   EXD, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9450936; DOI=10.1101/gad.12.3.435;
RA   Pai C.-Y., Kuo T.-S., Jaw T.J., Kurant E., Chen C.-T., Bessarab D.A.,
RA   Salzberg A., Sun Y.H.;
RT   "The Homothorax homeoprotein activates the nuclear localization of another
RT   homeoprotein, extradenticle, and suppresses eye development in
RT   Drosophila.";
RL   Genes Dev. 12:435-446(1998).
RN   [4] {ECO:0000312|EMBL:AAN13474.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAN13474.1};
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   [5] {ECO:0000305, ECO:0000312|EMBL:AAN13474.1}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
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   [6] {ECO:0000305, ECO:0000312|EMBL:ABC86272.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS E AND F).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:ABC86272.1}; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=14636555; DOI=10.1016/s0092-8674(03)00848-1;
RA   Wernet M.F., Labhart T., Baumann F., Mazzoni E.O., Pichaud F., Desplan C.;
RT   "Homothorax switches function of Drosophila photoreceptors from color to
RT   polarized light sensors.";
RL   Cell 115:267-279(2003).
RN   [8] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH EXD, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=16778079; DOI=10.1101/gad.1412606;
RA   Noro B., Culi J., McKay D.J., Zhang W., Mann R.S.;
RT   "Distinct functions of homeodomain-containing and homeodomain-less isoforms
RT   encoded by homothorax.";
RL   Genes Dev. 20:1636-1650(2006).
CC   -!- FUNCTION: All isoforms are required for patterning of the embryonic
CC       cuticle. Acts with exd to delimit the eye field and prevent
CC       inappropriate eye development. Isoforms that carry the homeodomain are
CC       required for proper localization of chordotonal organs within the
CC       peripheral nervous system and antennal identity; required to activate
CC       antennal-specific genes, such as sal and to repress the leg-like
CC       expression of dac. Necessary for the nuclear localization of the
CC       essential HOX cofactor, extradenticle (exd). Both necessary and
CC       sufficient for inner photoreceptors to adopt the polarization-sensitive
CC       'dorsal rim area' (DRA) of the eye fate instead of the color-sensitive
CC       default state. This occurs by increasing rhabdomere size and uncoupling
CC       R7-R8 communication to allow both cells to express the same opsin
CC       rather than different ones as required for color vision.
CC       {ECO:0000269|PubMed:14636555, ECO:0000269|PubMed:16778079,
CC       ECO:0000269|PubMed:9346235, ECO:0000269|PubMed:9450936,
CC       ECO:0000269|PubMed:9463350}.
CC   -!- SUBUNIT: Interacts with exd; required for nuclear translocation of exd.
CC       {ECO:0000269|PubMed:16778079, ECO:0000269|PubMed:9346235,
CC       ECO:0000269|PubMed:9450936, ECO:0000269|PubMed:9463350}.
CC   -!- INTERACTION:
CC       O46339; P40427: exd; NbExp=16; IntAct=EBI-137488, EBI-101537;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:9346235, ECO:0000269|PubMed:9450936,
CC       ECO:0000269|PubMed:9463350}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=C {ECO:0000269|PubMed:16778079, ECO:0000269|PubMed:9450936};
CC       Synonyms=hth1 {ECO:0000269|PubMed:9450936}, HthFL
CC       {ECO:0000269|PubMed:16778079};
CC         IsoId=O46339-1; Sequence=Displayed;
CC       Name=A {ECO:0000269|PubMed:9450936}; Synonyms=hth2
CC       {ECO:0000269|PubMed:9450936};
CC         IsoId=O46339-2; Sequence=VSP_052826;
CC       Name=E {ECO:0000269|PubMed:16778079}; Synonyms=HDless 7'
CC       {ECO:0000269|PubMed:16778079};
CC         IsoId=O46339-5; Sequence=VSP_052822, VSP_052824;
CC       Name=F {ECO:0000269|PubMed:16778079}; Synonyms=HDless 6'
CC       {ECO:0000269|PubMed:16778079}, I {ECO:0000312|FlyBase:FBgn0001235};
CC         IsoId=O46339-6; Sequence=VSP_052823, VSP_052824;
CC       Name=H {ECO:0000269|PubMed:9346235};
CC         IsoId=O46339-8; Sequence=VSP_052821, VSP_052826;
CC   -!- TISSUE SPECIFICITY: In the wing disk, the expression is present in the
CC       regions corresponding to notum, wing hinge and ventral pleura. In the
CC       leg disk, the expression is in the periphery region, corresponding to
CC       the proximal segments of the legs. In the antennal disk, the expression
CC       is in all but the arista region. In the eye disk, the expression is
CC       strong in the anterior region surrounding the eye field, including the
CC       regions corresponding to ptilinum, ocellus and head capsules, and weak
CC       in the posterior and lateral margins of the eye disk. Expressed
CC       specifically in maturating inner photoreceptors of the DRA and
CC       maintained through adulthood. {ECO:0000269|PubMed:14636555,
CC       ECO:0000269|PubMed:16778079, ECO:0000269|PubMed:9450936}.
CC   -!- DEVELOPMENTAL STAGE: Isoform C, isoform E and isoform F have very
CC       similar expression patterns during embryonic and larval stages,
CC       suggesting coexpression in the same tissues.
CC       {ECO:0000269|PubMed:16778079}.
CC   -!- DISRUPTION PHENOTYPE: Severe head defects, including a failure of head
CC       involution and transformation of the thoracic and abdominal segments
CC       into a more posterior identity. {ECO:0000269|PubMed:9346235}.
CC   -!- MISCELLANEOUS: [Isoform E]: Protein lacks the homeodomain but is still
CC       capable of interacting with exd. {ECO:0000269|PubMed:16778079}.
CC   -!- MISCELLANEOUS: [Isoform F]: Protein lacks the homeodomain but is still
CC       capable of interacting with exd. {ECO:0000269|PubMed:16778079}.
CC   -!- SIMILARITY: Belongs to the TALE/MEIS homeobox family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ23556.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF026788; AAC47759.1; -; mRNA.
DR   EMBL; AF032865; AAB97169.1; -; mRNA.
DR   EMBL; AF035825; AAB88514.1; -; mRNA.
DR   EMBL; AF036584; AAB88863.1; -; mRNA.
DR   EMBL; AE014297; AAF54533.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13474.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13475.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAX52943.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAZ52527.1; -; Genomic_DNA.
DR   EMBL; BT010238; AAQ23556.1; ALT_FRAME; mRNA.
DR   EMBL; BT024210; ABC86272.1; -; mRNA.
DR   EMBL; BT029117; ABJ17050.1; -; mRNA.
DR   RefSeq; NP_001014613.2; NM_001014613.3. [O46339-5]
DR   RefSeq; NP_001027170.1; NM_001031999.2. [O46339-6]
DR   RefSeq; NP_476576.1; NM_057228.5. [O46339-1]
DR   RefSeq; NP_476577.3; NM_057229.5. [O46339-6]
DR   RefSeq; NP_476578.3; NM_057230.6.
DR   AlphaFoldDB; O46339; -.
DR   SMR; O46339; -.
DR   BioGRID; 66419; 45.
DR   IntAct; O46339; 64.
DR   STRING; 7227.FBpp0081732; -.
DR   PaxDb; O46339; -.
DR   PRIDE; O46339; -.
DR   DNASU; 41273; -.
DR   EnsemblMetazoa; FBtr0082255; FBpp0081732; FBgn0001235. [O46339-1]
DR   EnsemblMetazoa; FBtr0100454; FBpp0099878; FBgn0001235. [O46339-5]
DR   EnsemblMetazoa; FBtr0100455; FBpp0099879; FBgn0001235. [O46339-6]
DR   EnsemblMetazoa; FBtr0344145; FBpp0310558; FBgn0001235. [O46339-6]
DR   GeneID; 41273; -.
DR   KEGG; dme:Dmel_CG17117; -.
DR   CTD; 41273; -.
DR   FlyBase; FBgn0001235; hth.
DR   VEuPathDB; VectorBase:FBgn0001235; -.
DR   eggNOG; KOG0773; Eukaryota.
DR   GeneTree; ENSGT00940000168996; -.
DR   InParanoid; O46339; -.
DR   OMA; PENNRAM; -.
DR   PhylomeDB; O46339; -.
DR   Reactome; R-DME-390193; Transcriptional activation by YKI.
DR   SignaLink; O46339; -.
DR   BioGRID-ORCS; 41273; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; hth; fly.
DR   GenomeRNAi; 41273; -.
DR   PRO; PR:O46339; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0001235; Expressed in wing disc and 72 other tissues.
DR   ExpressionAtlas; O46339; baseline and differential.
DR   Genevisible; O46339; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:FlyBase.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:FlyBase.
DR   GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0001752; P:compound eye photoreceptor fate commitment; IMP:FlyBase.
DR   GO; GO:0009880; P:embryonic pattern specification; IBA:GO_Central.
DR   GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR   GO; GO:0048735; P:haltere morphogenesis; IMP:FlyBase.
DR   GO; GO:0060323; P:head morphogenesis; IMP:FlyBase.
DR   GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0072002; P:Malpighian tubule development; IMP:FlyBase.
DR   GO; GO:0001742; P:oenocyte differentiation; IMP:FlyBase.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:2000497; P:positive regulation of cell proliferation involved in compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0034504; P:protein localization to nucleus; IPI:FlyBase.
DR   GO; GO:0009954; P:proximal/distal pattern formation; TAS:FlyBase.
DR   GO; GO:0042659; P:regulation of cell fate specification; IMP:FlyBase.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0007432; P:salivary gland boundary specification; TAS:FlyBase.
DR   GO; GO:0035282; P:segmentation; IMP:FlyBase.
DR   GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR   GO; GO:0010092; P:specification of animal organ identity; TAS:FlyBase.
DR   GO; GO:0007383; P:specification of segmental identity, antennal segment; IMP:FlyBase.
DR   GO; GO:0007380; P:specification of segmental identity, head; IMP:FlyBase.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR008422; Homeobox_KN_domain.
DR   InterPro; IPR032453; PKNOX/Meis_N.
DR   Pfam; PF05920; Homeobox_KN; 1.
DR   Pfam; PF16493; Meis_PKNOX_N; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; DNA-binding; Homeobox;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..487
FT                   /note="Homeobox protein homothorax"
FT                   /id="PRO_0000341484"
FT   DOMAIN          127..211
FT                   /note="MEIS N-terminal"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        365..427
FT                   /note="Homeobox; TALE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          25..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..14
FT                   /note="Missing (in isoform H)"
FT                   /evidence="ECO:0000303|PubMed:10731132,
FT                   ECO:0000303|PubMed:9346235"
FT                   /id="VSP_052821"
FT   VAR_SEQ         243..266
FT                   /note="RPPSSSLSYGGAMNDDARSPGAGS -> PSTQDFSPLEETYASYRIKHEADF
FT                   (in isoform E)"
FT                   /evidence="ECO:0000303|PubMed:16778079, ECO:0000303|Ref.6"
FT                   /id="VSP_052822"
FT   VAR_SEQ         243..266
FT                   /note="RPPSSSLSYGGAMNDDARSPGAGS -> VSTPFAGAHGPILASYNAVVHPCS
FT                   (in isoform F)"
FT                   /evidence="ECO:0000303|PubMed:16778079, ECO:0000303|Ref.6"
FT                   /id="VSP_052823"
FT   VAR_SEQ         267..487
FT                   /note="Missing (in isoform E and isoform F)"
FT                   /evidence="ECO:0000303|PubMed:16778079, ECO:0000303|Ref.6"
FT                   /id="VSP_052824"
FT   VAR_SEQ         284..398
FT                   /note="Missing (in isoform A and isoform H)"
FT                   /evidence="ECO:0000303|PubMed:10731132,
FT                   ECO:0000303|PubMed:9346235, ECO:0000303|PubMed:9450936,
FT                   ECO:0000303|Ref.6"
FT                   /id="VSP_052826"
SQ   SEQUENCE   487 AA;  52784 MW;  7EA4D7D1EFB16F8A CRC64;
     MAQPRYDDGL HGYGMDSGAA AAAMYDPHAG HRPPGLQGLP SHHSPHMTHA AAAAATVGMH
     GYHSGAGGHG TPSHVSPVGN HLMGAIPEVH KRDKDAIYEH PLFPLLALIF EKCELATCTP
     REPGVQGGDV CSSESFNEDI AMFSKQIRSQ KPYYTADPEV DSLMVQAIQV LRFHLLELEK
     VHELCDNFCH RYISCLKGKM PIDLVIDERD TTKPPELGSA NGEGRSNADS TSHTDGASTP
     DVRPPSSSLS YGGAMNDDAR SPGAGSTPGP LSQQPPALDT SDPDGKFLSS LNPSELTYDG
     RWCRREWSSP ADARNADASR RLYSSVFLGS PDNFGTSASG DASNASIGSG EGTGEEDDDA
     SGKKNQKKRG IFPKVATNIL RAWLFQHLTH PYPSEDQKKQ LAQDTGLTIL QVNNWFINAR
     RRIVQPMIDQ SNRAVYTPHP GPSGYGHDAM GYMMDSQAHM MHRPPGDPGF HQGYPHYPPA
     EYYGQHL
 
 
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