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BARK_DROME
ID   BARK_DROME              Reviewed;        3123 AA.
AC   M9NDE3; Q9VQV1;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Protein bark beetle {ECO:0000303|PubMed:25704509};
DE   AltName: Full=Protein anakonda {ECO:0000303|PubMed:25982676};
DE   Flags: Precursor;
GN   Name=bark {ECO:0000312|FlyBase:FBgn0031571};
GN   Synonyms=aka {ECO:0000303|PubMed:25982676};
GN   ORFNames=CG3921 {ECO:0000312|FlyBase:FBgn0031571};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=25704509; DOI=10.1016/j.ydbio.2015.02.008;
RA   Hildebrandt A., Pflanz R., Behr M., Tarp T., Riedel D., Schuh R.;
RT   "Bark beetle controls epithelial morphogenesis by septate junction
RT   maturation in Drosophila.";
RL   Dev. Biol. 400:237-247(2015).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP   CLEAVAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF VAL-503; VAL-567; GLU-678
RP   AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25982676; DOI=10.1016/j.devcel.2015.03.023;
RA   Byri S., Misra T., Syed Z.A., Baetz T., Shah J., Boril L., Glashauser J.,
RA   Aegerter-Wilmsen T., Matzat T., Moussian B., Uv A., Luschnig S.;
RT   "The triple-repeat protein anakonda controls epithelial tricellular
RT   junction formation in Drosophila.";
RL   Dev. Cell 33:535-548(2015).
CC   -!- FUNCTION: Required for the maturation but not the establishment of
CC       septate junctions in developing epithelial cells and is involved in
CC       epithelial cell adhesion during septate junction maturation
CC       (PubMed:25704509). Plays a role in the proper localization of the
CC       septate junction core components pck/mega, kune, Nrx-IV and Nrg during
CC       late embryogenesis (PubMed:25704509). Involved in the formation of
CC       tricellular junctions which mediate cell contact where three epithelial
CC       cells meet but not of bicellular junctions (PubMed:25982676). Required
CC       for the accumulation of Gli at tricellular junctions.
CC       {ECO:0000269|PubMed:25704509, ECO:0000269|PubMed:25982676}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000255}. Cell junction, septate junction
CC       {ECO:0000269|PubMed:25704509}. Cell junction, adherens junction
CC       {ECO:0000269|PubMed:25704509}. Cell junction, tight junction
CC       {ECO:0000269|PubMed:25982676}. Note=Found at tricellular contacts.
CC       {ECO:0000269|PubMed:25982676}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B {ECO:0000312|FlyBase:FBgn0031571};
CC         IsoId=M9NDE3-1; Sequence=Displayed;
CC       Name=A {ECO:0000312|FlyBase:FBgn0031571};
CC         IsoId=M9NDE3-2; Sequence=VSP_057995;
CC   -!- TISSUE SPECIFICITY: Expression detected in embryonic epithelia and
CC       central nervous system (at protein level) (PubMed:25982676). First
CC       detected during stage 13 in the tracheal system, the foregut, the
CC       hindgut, the salivary glands and the epidermis (PubMed:25704509,
CC       PubMed:25982676). Expression persists in these tissues until the end of
CC       embryogenesis (PubMed:25704509). Expression in epithelia declines from
CC       late stage 15 and expression appears in the central nervous system
CC       during stage 16 (PubMed:25982676). {ECO:0000269|PubMed:25704509,
CC       ECO:0000269|PubMed:25982676}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:25982676}.
CC   -!- PTM: May be proteolytically cleaved in the extracellular domain.
CC       {ECO:0000269|PubMed:25982676}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality. Mutant embryos establish
CC       functional septate junctions but, due to rudimentary septae formation
CC       during subsequent embryonic development, these become non-functional
CC       (PubMed:25704509). Abnormal liquid clearance of tracheal tubes
CC       (PubMed:25704509). Convoluted and elongated tracheal branches
CC       (PubMed:25704509, PubMed:25982676). During late embryogenesis,
CC       mislocalization of septate junction core components pck/mega, kune,
CC       Nrx-IV and Nrg and impaired cell adhesion at the lateral cell membrane
CC       (PubMed:25704509). Mislocalization of Fas3 in the epithelia of mutant
CC       embryos and loss of accumulation of Gli at tricellular junctions
CC       (PubMed:25982676). {ECO:0000269|PubMed:25704509,
CC       ECO:0000269|PubMed:25982676}.
CC   -!- MISCELLANEOUS: The name 'bark beetle' derives from the convoluted
CC       tracheal branches seen in mutant embryos which resemble the tracks of
CC       bark beetle larvae (PubMed:25704509). The name 'anakonda' is also based
CC       on the convoluted tracheal tube phenotype of mutant embryos
CC       (PubMed:25982676). {ECO:0000303|PubMed:25704509,
CC       ECO:0000303|PubMed:25982676}.
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DR   EMBL; AE014134; AAF51061.1; -; Genomic_DNA.
DR   EMBL; AE014134; AFH03540.1; -; Genomic_DNA.
DR   EMBL; AE014134; AFH03541.1; -; Genomic_DNA.
DR   RefSeq; NP_001245864.1; NM_001258935.3. [M9NDE3-1]
DR   RefSeq; NP_001245865.1; NM_001258936.2. [M9NDE3-1]
DR   RefSeq; NP_608808.1; NM_134964.4. [M9NDE3-2]
DR   SMR; M9NDE3; -.
DR   IntAct; M9NDE3; 3.
DR   STRING; 7227.FBpp0297894; -.
DR   GlyGen; M9NDE3; 38 sites.
DR   PaxDb; M9NDE3; -.
DR   PRIDE; M9NDE3; -.
DR   EnsemblMetazoa; FBtr0077496; FBpp0077185; FBgn0031571. [M9NDE3-2]
DR   EnsemblMetazoa; FBtr0307051; FBpp0297894; FBgn0031571. [M9NDE3-1]
DR   EnsemblMetazoa; FBtr0307052; FBpp0297895; FBgn0031571. [M9NDE3-1]
DR   GeneID; 33604; -.
DR   KEGG; dme:Dmel_CG3921; -.
DR   UCSC; CG3921-RA; d. melanogaster.
DR   CTD; 33604; -.
DR   FlyBase; FBgn0031571; bark.
DR   VEuPathDB; VectorBase:FBgn0031571; -.
DR   eggNOG; ENOG502QT9G; Eukaryota.
DR   HOGENOM; CLU_000296_1_0_1; -.
DR   OMA; MEFAPNV; -.
DR   PhylomeDB; M9NDE3; -.
DR   SignaLink; M9NDE3; -.
DR   BioGRID-ORCS; 33604; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33604; -.
DR   PRO; PR:M9NDE3; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031571; Expressed in insect embryonic/larval digestive system and 30 other tissues.
DR   Genevisible; Q9VQV1; DM.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
DR   GO; GO:0005918; C:septate junction; IDA:FlyBase.
DR   GO; GO:0061689; C:tricellular tight junction; IDA:FlyBase.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:FlyBase.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0045217; P:cell-cell junction maintenance; IMP:FlyBase.
DR   GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
DR   GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
DR   GO; GO:1904274; P:tricellular tight junction assembly; IMP:FlyBase.
DR   CDD; cd00041; CUB; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   Gene3D; 3.10.250.10; -; 3.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   Pfam; PF00530; SRCR; 3.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00710; PbH1; 19.
DR   SMART; SM00202; SR; 3.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   SUPFAM; SSF56487; SSF56487; 3.
DR   PROSITE; PS00420; SRCR_1; 1.
DR   PROSITE; PS50287; SRCR_2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Disulfide bond;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Tight junction;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..3123
FT                   /note="Protein bark beetle"
FT                   /id="PRO_5004101294"
FT   TOPO_DOM        35..2714
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        2715..2735
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2736..3123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          191..295
FT                   /note="SRCR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   REPEAT          358..380
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          382..404
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          406..428
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          446..559
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   REPEAT          562..584
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          586..609
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          611..633
FT                   /note="PbH1 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          756..778
FT                   /note="PbH1 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          789..809
FT                   /note="PbH1 8"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1071..1175
FT                   /note="SRCR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   REPEAT          1219..1241
FT                   /note="PbH1 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1248..1270
FT                   /note="PbH1 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1451..1475
FT                   /note="PbH1 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1489..1511
FT                   /note="PbH1 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1553..1575
FT                   /note="PbH1 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1722..1744
FT                   /note="PbH1 14"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1912..2037
FT                   /note="SRCR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   REPEAT          2104..2126
FT                   /note="PbH1 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2128..2150
FT                   /note="PbH1 16"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2337..2361
FT                   /note="PbH1 17"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2372..2393
FT                   /note="PbH1 18"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2401..2424
FT                   /note="PbH1 19"
FT                   /evidence="ECO:0000255"
FT   REGION          83..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2766..2789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2961..2983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2996..3015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3025..3123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2996..3013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3061..3087
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3104..3123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        615
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        630
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        639
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        672
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        702
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        709
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        834
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        900
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1040
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1520
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1614
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1883
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1920
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1940
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2596
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2636
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        216..284
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        231..294
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        262..272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        446..474
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DISULFID        1096..1164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        1109..1174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        1144..1154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        1950..2025
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        1963..2036
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        2000..2010
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   VAR_SEQ         2539..2547
FT                   /note="ILSFDYENR -> M (in isoform A)"
FT                   /id="VSP_057995"
FT   MUTAGEN         503
FT                   /note="V->E: In L224; embryonic lethality with excessively
FT                   elongated tracheal tubes."
FT                   /evidence="ECO:0000269|PubMed:25982676"
FT   MUTAGEN         567
FT                   /note="V->E: In J55; embryonic lethality with excessively
FT                   elongated tracheal tubes."
FT                   /evidence="ECO:0000269|PubMed:25982676"
FT   MUTAGEN         678
FT                   /note="E->K: In K93; embryonic lethality with excessively
FT                   elongated tracheal tubes."
FT                   /evidence="ECO:0000269|PubMed:25982676"
FT   MUTAGEN         680
FT                   /note="S->L: In K104; embryonic lethality with excessively
FT                   elongated tracheal tubes."
FT                   /evidence="ECO:0000269|PubMed:25982676"
SQ   SEQUENCE   3123 AA;  350461 MW;  3AB68B97DE35D73D CRC64;
     MKLQHHKTNR QRISKPHRDP KWASICLWLL VTLAFSTHLA RSQESRQTED SKEVELLQDN
     DIEFASLDGA SQLLPATRHS GADVTVAPQG STPSMTSSSS YTELQGGEIL SDRILRRSES
     PYLARDDIEV LRGARLTIEP GVTIEFAPTK GLKINGVLQA VGTPTSRIVL KSQSNTANYK
     LELPDDQEKG IRLVDGPTPV EGRLQLFHKG AWRSVCSNSR NWTLADYGVA CKQLGYRGGR
     FWNWVERTPG YYPRLLYEQP KCKGGEGSLQ DCAWTSRQMG AGACDYHNDL GIQCLPVHSE
     TLGHWRGIYF DNAPSTKALG RDNIVYAAQS ESRLKYVDII RAGSGAGFNA KSAVEVQGLP
     PQMEHVVISH SAYTGFNSTR PWAGFQLQNV TVRKCNGIGV FVNSSQGAVQ LDGCSIVDNA
     GDGIKYVGHD LRGTERKDRA SIYDFCTLPT TSGQTYPISL SFTQKYYAGS GKECGKYFFT
     RPGYLLTLHF ENFVLMQNET ATVEIYDGAS TNDRLLFEWK ARNFTRPQSV TSTREKMFVR
     IRADARQELN GFFRMTSGDS VAYDLKVSQS TVEDNGGRGV AIDNIRSKLH VHSSSVSGNG
     HVAGVHVTSG AGDVNITSSN ISFNNGAGVN ITYYGGNRNI SRSALTANKG YGVATWLNQT
     SDVNRMEYIP FNQTSVVEYS QIGGNLETGV FHGNFCRPIW VNITGNSFNG SQQNDIFIES
     CYQATANGRP NMQLQLGHNQ FKYSQANSIY LSPALNLQGR IEYNMFRFGS YGCLFINNDY
     IYPEFNYFPV KLIIQSNYFM RNSGVHVVSL GLSPYSRAEV QYILFTRNFV RGNNITEAFG
     PLIAGSEGSD GAGRLNPRSR VAAPVVVGSS NVDIFRNILH NLDSMYEIGS QLTDQSKIIN
     ATCNWLGHTD ENKIYARLFH RNDRYNLAKI NYLPYLLHSS NPGSTAMITV STVVPRFFHE
     GSDVIGGEVD GQDMVPAGTY TVTKDINIRP GGKLILQPGT TLKFEPSVGM MVAGKLEARG
     RRPDDILFTL KRETIMGESN DTETIDLDSE TEAIDMETEV IPADGVPRVP VRLVGGAGAN
     EGRLQVYLKG RWGTVCDYGW NVLNAALVCH QLGYSLNPQD WRLLRSQLPN AGTSEDILMA
     NVRCTLQDRD VTKCRAEYEF ENTCSHENDV GLRCYEGAWA GVRFSMLAER ADLQYVTVEK
     AGLFDYTTNA FKPAVQMDHA RHNLENVRIV NNLQDGLGII YADIYAGKSV NNIKNSEFSG
     NKGSGISLKQ LDFRVSGSII KDNKGSGVSH DAVISALDQK EIGGWFNMAT DFNSFDTDYD
     PYLLPREISN IDLGTFEHKY IRTEELLGQN INRKIVVQCP AGYVIGIQLL NPIHNLSTES
     INILNARTEN IRSDLWQVKR DLNVFPVTSS SYGIIIYYES GLQALGGAVL MLSTVTAPVQ
     NIRNRIVSGA VPTLTIRSTK IQKNLRGITG IYYNRYIGDN GEYYLRKANE SIKLINSELS
     YNEREAILIR SPFWDVISSN LSEVTLHVNG SLITQNGLGI RQMSKDLRSS NNLFHYVIQD
     TTFEQNTHGG FQVSLPYVWQ YNENFTHSIY FGNSTWQRNR DFRISVSGHY TVFNITSNVF
     RENNCPGALI SLDGMEKRLR FDNNRFESNN AKFVLLFKAD SLSEIIGQVP ASIEFNSFKG
     NNIVTMTANY RNHYMKVARR IRKQHKIPTA VIRLDGVQNV RLYRNLIAEN EMDYNLVAGV
     RSARLNNYFE ARENWWGTKD TAFIEAKIFD FDNWNDHADV IYQPFLIEDS YDASVSVVVP
     FNQDQEIDLT NYKGGRVYKD LLLTKQSTPY YISSDITVMP GKTLTINHGV TMEFEPNVGI
     LVLGTLVAIG YRESPIVMRP FRNATRESLI DVQPKKRALE DMSAPLTEFD SIRLCTSANN
     CTGDADGLFG LNEGFLEYFN HTTLQWVPIC DSRFTERNAQ VVCRELGYDP LNVYYGHDRR
     IEFHTNSLTR IWSWVQPLEC RGDEERMEDC AERLNGQLYG HRHECRWDDV FVFVSCNGIA
     DDEVYWGGIR FANSKFEEIQ YEHRLHNTRS HARLPLRESQ LEFVRIEQAG ILHNHKAAAI
     QAIHKNPSIT SVSIENSANH GINMIAPSGK LNLNHLNINN TLGTGISIVS LSGEGRDSDE
     SSFTPLKKLD LPYKLFSLVD ICDPQKVLTI EERMLIYYKY DNNPVNCVKI FTSAFRAKPI
     GFRLLQSNLF NHSKLYGRTD FIKLYDGDIY NVTATYLGKI ESDTDNQRSF FKTKGPTMSL
     QLVASGAPET HGFIAEVVTV PISTLGQYRD ALHNITDTHI SGAIKGAVTY SSAGEVTPTL
     TLIGNRIEKN CRQLYGNFST CTSALNLDVQ NMNSLYFMNN LITENQGGLR IRADSRGSAT
     SLRGFVHHNL FMRNRNRPAL YVEGRQSSPY QEVELYRNYF AQNMAGYEDV IRLCQVVSNF
     SYNYVHSNVG GRIMEVSGFE KVRLQIYQTT AHNGFYRNFA TNWMTRATIV AGTAGQQYVD
     NIFENHENDY ELLTVNNSIL SFDYENRTFE TWSSKIDARH NYWSYNNTIS VQSRIRDKSD
     DPMLLEVLAV PFQMNNETIL DGKCPPGWAL VHDTCFIYVG APMTFHEARD FCRSENSTMP
     FIRTDKTTLW KYLQSQMRHL KYPDKVWIQD YNHIDRCTSF VFGEIEIEDC NKERGFICES
     DPRVIIDPLS WRADIFAISI ISAFVLAIIL LILVAFCWFA KSKHRHTQRL QRRNSIRQSL
     RSLNSIDPQG SLRRRPNYNM SSNGTLSKGQ DYKQMVANGS IDSMDKSVLS SEAGSFEGYE
     QKPHYNEYVN QNALRPAHPA QDHQSHKVAT ISKASGHRAR AAAAAAAALE PDAFELSYRN
     EGFRDNSTYG DNTRANSIST SVAEDTPIIH HTDQEIDEGG SDYYGNASTL PLRTEGGTPA
     GRRGQPGLAF LSELKQNLPE YQRSSHSSFM PHRSSGDSLP FDQKLDQFNY STESSLYRPA
     PAVPSSQQAT PADMRRPDSY YTAVRSSKAP VSHYRTPRPL AQPPAAPNVA PAGGPAQRRP
     KTVYQTASEE SSPTTPSPLT NQYHRSKSEA LLETDFDGDG GSVGLQPLQT NGRSHSQPLE
     TAM
 
 
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