ID Q9W4T9_DROME Unreviewed; 956 AA.
AC Q9W4T9;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 2.
DT 27-MAR-2024, entry version 195.
DE SubName: Full=Kin of irre, isoform A {ECO:0000313|EMBL:AAF45847.2};
DE SubName: Full=Kin of irre, isoform B {ECO:0000313|EMBL:AAN09598.1};
DE SubName: Full=Kin of irre, isoform C {ECO:0000313|EMBL:AFH07219.1};
DE SubName: Full=Kin of irre, isoform D {ECO:0000313|EMBL:AFH07220.1};
DE SubName: Full=Kin of irre, isoform E {ECO:0000313|EMBL:AFH07221.1};
DE SubName: Full=Kin of irre, isoform F {ECO:0000313|EMBL:AFH07222.1};
DE SubName: Full=Kin of irre, isoform G {ECO:0000313|EMBL:AGB95042.1};
GN Name=kirre {ECO:0000313|EMBL:AAF45847.2,
GN ECO:0000313|FlyBase:FBgn0028369};
GN Synonyms=CT12279 {ECO:0000313|EMBL:AAF45847.2}, Dmel\CG3653
GN {ECO:0000313|EMBL:AAF45847.2}, DUF {ECO:0000313|EMBL:AAF45847.2}, Duf
GN {ECO:0000313|EMBL:AAF45847.2}, duf {ECO:0000313|EMBL:AAF45847.2},
GN DUF/KIRRE {ECO:0000313|EMBL:AAF45847.2}, Duf/Kirre
GN {ECO:0000313|EMBL:AAF45847.2}, duf/kirre
GN {ECO:0000313|EMBL:AAF45847.2}, EG:163A10.1
GN {ECO:0000313|EMBL:AAF45847.2}, Kirre {ECO:0000313|EMBL:AAF45847.2},
GN RH09239 {ECO:0000313|EMBL:AAF45847.2};
GN ORFNames=CG3653 {ECO:0000313|EMBL:AAF45847.2,
GN ECO:0000313|FlyBase:FBgn0028369}, Dmel_CG3653
GN {ECO:0000313|EMBL:AAF45847.2};
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:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|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 [4] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AAF45847.2}
RP NUCLEOTIDE SEQUENCE.
RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA Svirskas R., Rubin G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [9] {ECO:0000313|EMBL:AAF45847.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
RN [10] {ECO:0007829|PDB:4OFI}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 81-185, GLYCOSYLATION AT ASN-126,
RP AND DISULFIDE BONDS.
RX PubMed=24485456; DOI=10.1016/j.cell.2014.01.004;
RA Ozkan E., Chia P.H., Wang R.R., Goriatcheva N., Borek D., Otwinowski Z.,
RA Walz T., Shen K., Garcia K.C.;
RT "Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs
RT synaptogenesis.";
RL Cell 156:482-494(2014).
RN [11] {ECO:0000313|EMBL:AAF45847.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109357; DOI=.1534/g3.115.018929;
RG FlyBase Consortium;
RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA Gelbart W.M., null;
RT "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT Throughput Data.";
RL G3 (Bethesda) 5:1721-1736(2015).
RN [12] {ECO:0000313|EMBL:AAF45847.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109356; DOI=.1534/g3.115.018937;
RG FlyBase Consortium;
RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA null;
RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL G3 (Bethesda) 5:1737-1749(2015).
RN [13] {ECO:0000313|EMBL:AAF45847.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25589440;
RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA Karpen G.H., Celniker S.E.;
RT "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL Genome Res. 25:445-458(2015).
RN [14] {ECO:0000313|EMBL:AAF45847.2}
RP NUCLEOTIDE SEQUENCE.
RG Berkeley Drosophila Genome Project;
RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA Rubin G.;
RT "Drosophila melanogaster release 4 sequence.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [15] {ECO:0000313|EMBL:AAF45847.2}
RP NUCLEOTIDE SEQUENCE.
RG FlyBase;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; AE014298; AAF45847.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09598.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07219.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07220.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07221.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07222.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95042.1; -; Genomic_DNA.
DR RefSeq; NP_001245505.1; NM_001258576.1.
DR RefSeq; NP_001245506.1; NM_001258577.1.
DR RefSeq; NP_001245507.1; NM_001258578.1.
DR RefSeq; NP_001245508.1; NM_001258579.3.
DR RefSeq; NP_001259196.1; NM_001272267.1.
DR RefSeq; NP_525059.2; NM_080320.4.
DR RefSeq; NP_726844.1; NM_166958.2.
DR PDB; 4OFI; X-ray; 2.30 A; A/B/C/D/E/F/G/H=81-185.
DR PDBsum; 4OFI; -.
DR ComplexPortal; CPX-2991; kirre cell adhesion complex.
DR ComplexPortal; CPX-2999; hbs-kirre cell adhesion complex.
DR ComplexPortal; CPX-3000; hbs-sns cell adhesion complex.
DR IntAct; Q9W4T9; 1.
DR STRING; 7227.FBpp0301281; -.
DR PaxDb; 7227-FBpp0301280; -.
DR EnsemblMetazoa; FBtr0070559; FBpp0070534; FBgn0028369.
DR EnsemblMetazoa; FBtr0070560; FBpp0070535; FBgn0028369.
DR EnsemblMetazoa; FBtr0309498; FBpp0301278; FBgn0028369.
DR EnsemblMetazoa; FBtr0309499; FBpp0301279; FBgn0028369.
DR EnsemblMetazoa; FBtr0309500; FBpp0301280; FBgn0028369.
DR EnsemblMetazoa; FBtr0309501; FBpp0301281; FBgn0028369.
DR EnsemblMetazoa; FBtr0332492; FBpp0304768; FBgn0028369.
DR GeneID; 31292; -.
DR KEGG; dme:Dmel_CG3653; -.
DR UCSC; CG3653-RA; d. melanogaster.
DR AGR; FB:FBgn0028369; -.
DR CTD; 31292; -.
DR FlyBase; FBgn0028369; kirre.
DR VEuPathDB; VectorBase:FBgn0028369; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000168476; -.
DR HOGENOM; CLU_013520_2_0_1; -.
DR OMA; HNVTRQY; -.
DR OrthoDB; 5362512at2759; -.
DR Reactome; R-DME-373753; Nephrin family interactions.
DR BioGRID-ORCS; 31292; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31292; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0028369; Expressed in dorsal pharyngeal muscle primordium (Drosophila) and 21 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005917; C:nephrocyte diaphragm; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IPI:ComplexPortal.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; NAS:ComplexPortal.
DR GO; GO:0008407; P:chaeta morphogenesis; IGI:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IDA:ComplexPortal.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; NAS:ComplexPortal.
DR GO; GO:0036058; P:filtration diaphragm assembly; IMP:FlyBase.
DR GO; GO:0061321; P:garland nephrocyte differentiation; IMP:FlyBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:ComplexPortal.
DR GO; GO:0007523; P:larval visceral muscle development; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0036059; P:nephrocyte diaphragm assembly; IMP:FlyBase.
DR GO; GO:0097206; P:nephrocyte filtration; IMP:FlyBase.
DR GO; GO:1901739; P:regulation of myoblast fusion; IDA:ComplexPortal.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; IDA:ComplexPortal.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11640:SF153; IRREGULAR CHIASM C-ROUGHEST PROTEIN-RELATED; 1.
DR PANTHER; PTHR11640; NEPHRIN; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4OFI};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..956
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015100932"
FT TRANSMEM 570..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..181
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 186..284
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 291..379
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 382..446
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 452..560
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 33..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 126
FT /note="N-acetyl-D-glucosamine"
FT /evidence="ECO:0007829|PDB:4OFI"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:4OFI"
FT DISULFID 103..161
FT /evidence="ECO:0007829|PDB:4OFI"
SQ SEQUENCE 956 AA; 101109 MW; 3E8AE918C8EF77D8 CRC64;
MKRMRSSRLL VLPLILVLIL TLLLQPIAVH AKSKKNKSSQ SSHHGDSSSS SSSSSSSSGS
SSAAASSAND ESKPKGGDNG GQHFAMEPQD QTAVVGSRVT LPCRVMEKVG ALQWTKDDFG
LGQHRNLSGF ERYSMVGSDE EGDFSLDIYP LMLDDDAKYQ CQVGPGPQGE QGIRSRFAKL
TVLVPPEAPK ITQGDYLVTT EDREIELECV SQGGKPAAEI TWIDGLGNVL TKGIEYVKEP
LADSRRITAR SILKLAPKKE HHNTTFTCQA QNTADRTYRS AKLLLEVKYA PKVIVSVVGG
ALAGGKIPEG AEVILSCQAD ANPHELSYRW FINDELMTGD FTTKMIIHNV SRQYHDAIVK
CEVVNAVGKS EQSKKLDISF GPVFRQRPVS VEADLGATVS MRCDVAGNPE PEIEWISENS
DQVVGVAAEL KLKVSSETAG RYFCKAVVNG FPEIGAEATL YVKRAPIITS HKVQFGGVGG
RVKIDCLAFS IPKAEHILWS FEGKIINMSS ADPDIYIFEE HHLPEGVRAA LIIRDSKATH
FGKYNCTVMN SYGGDSLVIT LLREPGNIPV LLVVMGSMFC VAIILMIVMI IIVYRKRRSR
KKPMPADVIP EASRGGDKLN ELKSELRSKA YDVEYSEAGG DGLAINLTQS PMPDVQMKGA
TLGVPLAGPV KFDERFSGDF GGDRYNRQCH IKNLKNQQET AYKGSPQANG YAHYFEYALD
YSPPGGEGAA VVVGSGGVGK LKNGGMNSAT LPHSAAATVN GGGAGNGGGA SLPRNQRHEI
QQSQQSNGFL GQPLLQNGID SRFSAIYGNP YLRTNSSLLP PLPPPSTANP AATPAPPPYH
AARHGHAHHA NGGLKHFVGG AVITTSPVGN VNINGGGGGG STPSGGGGVG VGVAAGGSVS
GSSSNLTASS NTLAATPLAG GGVGNSGQCA QSPSGQFILS NNGKGHTQKG PLATHV
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