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Protein bark beetle (Protein anakonda)

 BARK_DROME              Reviewed;        3123 AA.
M9NDE3; Q9VQV1;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 1.
16-JAN-2019, entry version 53.
RecName: Full=Protein bark beetle {ECO:0000303|PubMed:25704509};
AltName: Full=Protein anakonda {ECO:0000303|PubMed:25982676};
Flags: Precursor;
Name=bark {ECO:0000312|FlyBase:FBgn0031571};
Synonyms=aka {ECO:0000303|PubMed:25982676};
ORFNames=CG3921 {ECO:0000312|FlyBase:FBgn0031571};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=25704509; DOI=10.1016/j.ydbio.2015.02.008;
Hildebrandt A., Pflanz R., Behr M., Tarp T., Riedel D., Schuh R.;
"Bark beetle controls epithelial morphogenesis by septate junction
maturation in Drosophila.";
Dev. Biol. 400:237-247(2015).
[4] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION,
CLEAVAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF VAL-503; VAL-567;
GLU-678 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25982676; DOI=10.1016/j.devcel.2015.03.023;
Byri S., Misra T., Syed Z.A., Baetz T., Shah J., Boril L.,
Glashauser J., Aegerter-Wilmsen T., Matzat T., Moussian B., Uv A.,
Luschnig S.;
"The triple-repeat protein anakonda controls epithelial tricellular
junction formation in Drosophila.";
Dev. Cell 33:535-548(2015).
-!- FUNCTION: Required for the maturation but not the establishment of
septate junctions in developing epithelial cells and is involved
in epithelial cell adhesion during septate junction maturation
(PubMed:25704509). Plays a role in the proper localization of the
septate junction core components pck/mega, kune, Nrx-IV and Nrg
during late embryogenesis (PubMed:25704509). Involved in the
formation of tricellular junctions which mediate cell contact
where three epithelial cells meet but not of bicellular junctions
(PubMed:25982676). Required for the accumulation of Gli at
tricellular junctions. {ECO:0000269|PubMed:25704509,
ECO:0000269|PubMed:25982676}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000255}. Cell junction, septate
junction {ECO:0000269|PubMed:25704509}. Cell junction, adherens
junction {ECO:0000269|PubMed:25704509}. Cell junction, tight
junction {ECO:0000269|PubMed:25982676}. Note=Found at tricellular
contacts. {ECO:0000269|PubMed:25982676}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B {ECO:0000312|FlyBase:FBgn0031571};
IsoId=M9NDE3-1; Sequence=Displayed;
Note=Gene prediction based on EST data. {ECO:0000305};
Name=A {ECO:0000312|FlyBase:FBgn0031571};
IsoId=M9NDE3-2; Sequence=VSP_057995;
Note=Gene prediction based on EST data. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expression detected in embryonic epithelia and
central nervous system (at protein level) (PubMed:25982676). First
detected during stage 13 in the tracheal system, the foregut, the
hindgut, the salivary glands and the epidermis (PubMed:25704509,
PubMed:25982676). Expression persists in these tissues until the
end of embryogenesis (PubMed:25704509). Expression in epithelia
declines from late stage 15 and expression appears in the central
nervous system during stage 16 (PubMed:25982676).
{ECO:0000269|PubMed:25704509, ECO:0000269|PubMed:25982676}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:25982676}.
-!- PTM: May be proteolytically cleaved in the extracellular domain.
{ECO:0000269|PubMed:25982676}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality. Mutant embryos
establish functional septate junctions but, due to rudimentary
septae formation during subsequent embryonic development, these
become non-functional (PubMed:25704509). Abnormal liquid clearance
of tracheal tubes (PubMed:25704509). Convoluted and elongated
tracheal branches (PubMed:25704509, PubMed:25982676). During late
embryogenesis, mislocalization of septate junction core components
pck/mega, kune, Nrx-IV and Nrg and impaired cell adhesion at the
lateral cell membrane (PubMed:25704509). Mislocalization of Fas3
in the epithelia of mutant embryos and loss of accumulation of Gli
at tricellular junctions (PubMed:25982676).
{ECO:0000269|PubMed:25704509, ECO:0000269|PubMed:25982676}.
-!- MISCELLANEOUS: The name 'bark beetle' derives from the convoluted
tracheal branches seen in mutant embryos which resemble the tracks
of bark beetle larvae (PubMed:25704509). The name 'anakonda' is
also based on the convoluted tracheal tube phenotype of mutant
embryos (PubMed:25982676). {ECO:0000303|PubMed:25704509,
ECO:0000303|PubMed:25982676}.
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EMBL; AE014134; AAF51061.1; -; Genomic_DNA.
EMBL; AE014134; AFH03540.1; -; Genomic_DNA.
EMBL; AE014134; AFH03541.1; -; Genomic_DNA.
RefSeq; NP_001245864.1; NM_001258935.3. [M9NDE3-1]
RefSeq; NP_001245865.1; NM_001258936.2. [M9NDE3-1]
RefSeq; NP_608808.1; NM_134964.4. [M9NDE3-2]
SMR; M9NDE3; -.
IntAct; M9NDE3; 3.
PaxDb; M9NDE3; -.
PRIDE; M9NDE3; -.
EnsemblMetazoa; FBtr0077496; FBpp0077185; FBgn0031571. [M9NDE3-2]
EnsemblMetazoa; FBtr0307051; FBpp0297894; FBgn0031571. [M9NDE3-1]
EnsemblMetazoa; FBtr0307052; FBpp0297895; FBgn0031571. [M9NDE3-1]
GeneID; 33604; -.
KEGG; dme:Dmel_CG3921; -.
UCSC; CG3921-RA; d. melanogaster.
CTD; 33604; -.
FlyBase; FBgn0031571; bark.
eggNOG; ENOG410IFUC; Eukaryota.
eggNOG; ENOG410XPY8; LUCA.
OMA; NHIERCT; -.
PhylomeDB; M9NDE3; -.
GenomeRNAi; 33604; -.
PRO; PR:M9NDE3; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0031571; Expressed in 32 organ(s), highest expression level in imaginal disc.
Genevisible; Q9VQV1; DM.
GO; GO:0005912; C:adherens junction; IDA:FlyBase.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005918; C:septate junction; IDA:FlyBase.
GO; GO:0061689; C:tricellular tight junction; IDA:FlyBase.
GO; GO:0030246; F:carbohydrate binding; ISS:FlyBase.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0045217; P:cell-cell junction maintenance; IMP:FlyBase.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:FlyBase.
GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
GO; GO:1904274; P:tricellular tight junction assembly; IMP:FlyBase.
CDD; cd00041; CUB; 1.
Gene3D; 2.60.120.290; -; 1.
Gene3D; 3.10.100.10; -; 1.
Gene3D; 3.10.250.10; -; 3.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000859; CUB_dom.
InterPro; IPR006626; PbH1.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
Pfam; PF00530; SRCR; 3.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00710; PbH1; 19.
SMART; SM00202; SR; 3.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF51126; SSF51126; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF56487; SSF56487; 3.
PROSITE; PS00420; SRCR_1; 1.
PROSITE; PS50287; SRCR_2; 3.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat;
Signal; Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 3123 Protein bark beetle.
/FTId=PRO_5004101294.
TOPO_DOM 35 2714 Extracellular. {ECO:0000305}.
TRANSMEM 2715 2735 Helical. {ECO:0000255}.
TOPO_DOM 2736 3123 Cytoplasmic. {ECO:0000305}.
DOMAIN 191 295 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
REPEAT 358 380 PbH1 1. {ECO:0000255}.
REPEAT 382 404 PbH1 2. {ECO:0000255}.
REPEAT 406 428 PbH1 3. {ECO:0000255}.
DOMAIN 446 559 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
REPEAT 562 584 PbH1 4. {ECO:0000255}.
REPEAT 586 609 PbH1 5. {ECO:0000255}.
REPEAT 611 633 PbH1 6. {ECO:0000255}.
REPEAT 756 778 PbH1 7. {ECO:0000255}.
REPEAT 789 809 PbH1 8. {ECO:0000255}.
DOMAIN 1071 1175 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
REPEAT 1219 1241 PbH1 9. {ECO:0000255}.
REPEAT 1248 1270 PbH1 10. {ECO:0000255}.
REPEAT 1451 1475 PbH1 11. {ECO:0000255}.
REPEAT 1489 1511 PbH1 12. {ECO:0000255}.
REPEAT 1553 1575 PbH1 13. {ECO:0000255}.
REPEAT 1722 1744 PbH1 14. {ECO:0000255}.
DOMAIN 1912 2037 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
REPEAT 2104 2126 PbH1 15. {ECO:0000255}.
REPEAT 2128 2150 PbH1 16. {ECO:0000255}.
REPEAT 2337 2361 PbH1 17. {ECO:0000255}.
REPEAT 2372 2393 PbH1 18. {ECO:0000255}.
REPEAT 2401 2424 PbH1 19. {ECO:0000255}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 523 523 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 620 620 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 639 639 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 658 658 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 672 672 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 702 702 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 709 709 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 834 834 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 900 900 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1040 1040 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1375 1375 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1489 1489 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1520 1520 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1529 1529 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1584 1584 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1593 1593 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1614 1614 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1883 1883 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1920 1920 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1940 1940 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2139 2139 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2231 2231 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2251 2251 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2314 2314 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2357 2357 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2459 2459 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2536 2536 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2546 2546 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2566 2566 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2596 2596 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2636 2636 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 216 284 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 231 294 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 262 272 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 446 474 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 1096 1164 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 1109 1174 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 1144 1154 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 1950 2025 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 1963 2036 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 2000 2010 {ECO:0000255|PROSITE-ProRule:PRU00196}.
VAR_SEQ 2539 2547 ILSFDYENR -> M (in isoform A).
/FTId=VSP_057995.
MUTAGEN 503 503 V->E: In L224; embryonic lethality with
excessively elongated tracheal tubes.
{ECO:0000269|PubMed:25982676}.
MUTAGEN 567 567 V->E: In J55; embryonic lethality with
excessively elongated tracheal tubes.
{ECO:0000269|PubMed:25982676}.
MUTAGEN 678 678 E->K: In K93; embryonic lethality with
excessively elongated tracheal tubes.
{ECO:0000269|PubMed:25982676}.
MUTAGEN 680 680 S->L: In K104; embryonic lethality with
excessively elongated tracheal tubes.
{ECO:0000269|PubMed:25982676}.
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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84650-55-5 Buckthorn Bark Buckthorn Bark 1g
3579 SPECIFIC IgE BERLIN BEETLE (Trogoderma angustum), SERUM 1
A-6401-1 Allomyrina dichotoma Lectin (Japanese Beetle) _Allo A_, 1mg 1mL
8011-48-1 Pine Bark Extract Pine Bark Extract 1g
R-6401-1 TRITC Conjugated Allomyrina dichotoma Lectin (Japanese Beetle) _Allo A_, 1mg 1mg
DY649-6401-1 DyLight649 Conjugated Allomyrina dichotoma Lectin (Japanese Beetle) _Allo A_, 1mg 1mg
DY488-6401-1 DyLight488 Conjugated Allomyrina dichotoma Lectin (Japanese Beetle) _Allo A_, 1mg 1mg
DY549-6401-1 DyLight549 Conjugated Allomyrina dichotoma Lectin (Japanese Beetle) _Allo A_, 1mg 1mg
H-6802-1 HRP Conjugated Sambucus nigra (Elderberry Bark) _SNA_I_, 1mg 1mg
L-6802-2 Pure Sambucus nigra (Elderberry Bark) _SNA_I_, 2mg 2mg
L-6803-5 Pure Sambucus nigra (Elderberry Bark) _SNA_II_, 5mg 5mg
H-6803-1 HRP Conjugated Sambucus nigra (Elderberry Bark) _SNA_II_, 1mg 1mg
L-6802-5 Pure Sambucus nigra (Elderberry Bark) _SNA_I_, 5mg 5mg
L-6803-2 Pure Sambucus nigra (Elderberry Bark) _SNA_II_, 2mg 2mg
R-6803-1 TRITC Conjugated Sambucus nigra (Elderberry Bark) _SNA_II_, 1mg 1mg
T-6802-1 Texas Red Conjugated Sambucus nigra (Elderberry Bark) _SNA_I_, 1mg 1mg
R-6802-1 TRITC Conjugated Sambucus nigra (Elderberry Bark) _SNA_I_, 1mg 1mg
F-6803-1 FITC Conjugated Sambucus nigra (Elderberry Bark) _SNA_II_, 1mg 1mg
T-6803-1 Texas Red Conjugated Sambucus nigra (Elderberry Bark) _SNA_II_, 1mg 1mg
R-6801-1 TRITC Conjugated Sambucus nigra (Elderberry Bark) _SNA_, 1mg 1mg
F-6802-1 FITC Conjugated Sambucus nigra (Elderberry Bark) _SNA_I_, 1mg 1mg
BA-6802-1 Biotin Conjugated Sambucus nigra (Elderberry Bark) _SNA_I_, 1mg 1mg
BA-6803-1 Biotin Conjugated Sambucus nigra (Elderberry Bark) _SNA_II_, 1mg 1mg
LA-6803-1 Alkaline Phosphatase Conjugated Sambucus nigra (Elderberry Bark) _SNA_II_, 1mg 1mg
LA-6802-1 Alkaline Phosphatase Conjugated Sambucus nigra (Elderberry Bark) _SNA_I_, 1mg 1mg

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[TMK4 BARK1 At3g23750 MYM9.9] Receptor-like kinase TMK4 (EC 2.7.11.1) (BAK1-associating receptor-like kinase 1) (Leucine-rich repeat receptor-like kinases TMK4) (Transmembrane kinase 4)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[OR1D2 OLFR1] Olfactory receptor 1D2 (Olfactory receptor 17-4) (OR17-4) (Olfactory receptor OR17-6) (Olfactory receptor-like protein HGMP07E)
[stk-1 bur1 B20D17.070 NCU01435] Serine/threonine-protein kinase bur1 (EC 2.7.11.22) (EC 2.7.11.23) (Serine-threonine kinase 1)
[frq B13D24.170 NCU02265] Frequency clock protein
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[cat-1 NCU08791] Catalase-1 (EC 1.11.1.6)
[OR1F1 OLFMF OR1F10 OR1F4 OR1F5 OR1F6 OR1F7 OR1F8 OR1F9] Olfactory receptor 1F1 (Olfactory receptor 16-35) (OR16-35) (Olfactory receptor 1F10) (Olfactory receptor 1F4) (Olfactory receptor 1F5) (Olfactory receptor 1F6) (Olfactory receptor 1F7) (Olfactory receptor 1F8) (Olfactory receptor 1F9) (Olfactory receptor OR16-4)
[TY1B-OR YORWTy1-2 POL YOR142W-B O3367 YOR3367W] Transposon Ty1-OR Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
[TY2B-OR2 YORWTy2-2 POL YOR343W-B O6304] Transposon Ty2-OR2 Gag-Pol polyprotein (TY2A-TY2B) (Transposon Ty2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA); Ty2 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)]
[scon-2 B13M15.090 NCU08563] Probable E3 ubiquitin ligase complex SCF subunit scon-2 (Sulfur controller 2) (SCON2) (Sulfur metabolite repression control protein 2)
[OR7D4 OR7D4P] Olfactory receptor 7D4 (OR19-B) (Odorant receptor family subfamily D member 4RT) (Olfactory receptor OR19-7)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Ubiquinol-cytochrome-c reductase complex core protein I)
[TY2B-OR1 YORCTy2-1 POL YOR192C-B O4785] Transposon Ty2-OR1 Gag-Pol polyprotein (TY2A-TY2B) (Transposon Ty2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA); Ty2 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)]
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Kmt2a All1 Hrx Mll Mll1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[T 90C4.150 NCU00776] Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase)
[cfp pdc-1 NCU02193] Pyruvate decarboxylase (EC 4.1.1.1) (8-10 nm cytoplasmic filament-associated protein) (P59NC)
[NCU03947] E3 ubiquitin-protein ligase (EC 2.3.2.26)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[cyt-18 B18P24.070 NCU03030] Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS)
[glmU OR1_01412] Bifunctional protein GlmU [Includes: Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157); UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase)]
[ppnP OR1_03385] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[ribA ribB OR37_01047] Multifunctional fusion protein [Includes: GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II); 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12)]
[nnr nnrD nnrE OR1_02963] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[OR3A3 OR3A6 OR3A7 OR3A8P] Olfactory receptor 3A3 (Olfactory receptor 17-201) (OR17-201) (Olfactory receptor 3A6) (Olfactory receptor 3A7) (Olfactory receptor 3A8) (Olfactory receptor OR17-22)

Bibliography :
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