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Database: UniProt
Entry: Q9VW34_DROME
LinkDB: Q9VW34_DROME
Original site: Q9VW34_DROME 
ID   Q9VW34_DROME            Unreviewed;       541 AA.
AC   Q9VW34;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 2.
DT   24-JAN-2024, entry version 185.
DE   SubName: Full=FI03450p {ECO:0000313|EMBL:ACM78483.1};
DE   SubName: Full=Serpentine, isoform B {ECO:0000313|EMBL:AAF49119.2};
DE   SubName: Full=Serpentine, isoform C {ECO:0000313|EMBL:AGB94755.1};
DE            EC=3.5.1.41 {ECO:0000313|EMBL:AAF49119.2, ECO:0000313|EMBL:AGB94755.1};
GN   Name=serp {ECO:0000313|EMBL:AAF49119.2,
GN   ECO:0000313|FlyBase:FBgn0260653};
GN   Synonyms=CG8747 {ECO:0000313|EMBL:AAF49119.2}, CG8748
GN   {ECO:0000313|EMBL:AAF49119.2}, DmCDA1 {ECO:0000313|EMBL:AAF49119.2},
GN   Dmel\CG32209 {ECO:0000313|EMBL:AAF49119.2}, l(3)76BDk
GN   {ECO:0000313|EMBL:AAF49119.2}, Serp {ECO:0000313|EMBL:AAF49119.2},
GN   serp-RB {ECO:0000313|EMBL:ACM78483.1};
GN   ORFNames=CG32209 {ECO:0000313|EMBL:AAF49119.2,
GN   ECO:0000313|FlyBase:FBgn0260653}, Dmel_CG32209
GN   {ECO:0000313|EMBL:AAF49119.2};
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:AAF49119.2, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAF49119.2, 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|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|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|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:AAF49119.2, 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:AAF49119.2, 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:AAF49119.2}
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:AAF49119.2, 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:AAF49119.2, 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:0000313|EMBL:ACM78483.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|EMBL:AAF49119.2}
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:AAF49119.2}
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:AAF49119.2}
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:AAF49119.2}
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 (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [15] {ECO:0000313|EMBL:AAF49119.2}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AE014296; AAF49119.2; -; Genomic_DNA.
DR   EMBL; BT058041; ACM78483.1; -; mRNA.
DR   EMBL; AE014296; AGB94755.1; -; Genomic_DNA.
DR   RefSeq; NP_001262062.1; NM_001275133.1.
DR   RefSeq; NP_730444.1; NM_168811.2.
DR   AlphaFoldDB; Q9VW34; -.
DR   SMR; Q9VW34; -.
DR   IntAct; Q9VW34; 2.
DR   STRING; 7227.FBpp0074721; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GlyGen; Q9VW34; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0074721; -.
DR   EnsemblMetazoa; FBtr0074953; FBpp0074721; FBgn0260653.
DR   EnsemblMetazoa; FBtr0333862; FBpp0305995; FBgn0260653.
DR   GeneID; 40150; -.
DR   KEGG; dme:Dmel_CG32209; -.
DR   UCSC; CG32209-RB; d. melanogaster.
DR   AGR; FB:FBgn0260653; -.
DR   CTD; 40150; -.
DR   FlyBase; FBgn0260653; serp.
DR   VEuPathDB; VectorBase:FBgn0260653; -.
DR   eggNOG; ENOG502QQP5; Eukaryota.
DR   HOGENOM; CLU_022576_1_0_1; -.
DR   InParanoid; Q9VW34; -.
DR   OMA; TCDWKDS; -.
DR   OrthoDB; 4572257at2759; -.
DR   BioGRID-ORCS; 40150; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; serp; fly.
DR   GenomeRNAi; 40150; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0260653; Expressed in capitellum (Drosophila) and 26 other cell types or tissues.
DR   ExpressionAtlas; Q9VW34; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:0062129; C:chitin-based extracellular matrix; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0005770; C:late endosome; IDA:FlyBase.
DR   GO; GO:0008061; F:chitin binding; IMP:FlyBase.
DR   GO; GO:0004099; F:chitin deacetylase activity; IMP:FlyBase.
DR   GO; GO:0008365; P:adult chitin-based cuticle development; IMP:FlyBase.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR   GO; GO:0006034; P:cuticle chitin metabolic process; IMP:FlyBase.
DR   GO; GO:0008363; P:larval chitin-based cuticle development; IMP:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR   CDD; cd10974; CE4_CDA_like_1; 1.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR45985; -; 1.
DR   PANTHER; PTHR45985:SF6; FI03450P; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Hydrolase {ECO:0000313|EMBL:AAF49119.2};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9VW34};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..541
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015100688"
FT   DOMAIN          45..107
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DISULFID        125..137
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        132..150
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        144..159
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   541 AA;  61609 MW;  5312DF686B7F28AD CRC64;
     MAKLFVVFAV LALAAFNEAS ASDPLLRYKR QATTEETKKE ESFEKELCKD KDAGEWFRLV
     AGEGDNCRDV IQCTSSGLQA IRCPAGLYFD IEKQTCDWKE SVKNCKSKNK ERRVKPLLHT
     DEPLCQDGFL ACGDGNCIER GLFCNGEKDC SDGSDENTCD IDNDPNRAPP CDPAVCVLPD
     CFCSEDGTSI PGDLPAKDVP MMITITFDDA INNNNIELYK EIFKDRKNPN GCSIKATYFV
     SHKYTNYSAV QETARKGHEI AVHSITHNDE ERFWSNATVD DWAKEMAGMR IITEKFANIT
     DNSVVGVRAP YLRVGGNNQF TMMEEQAFLY DSTITAPLSN PPLWPYTMYF RMPHRCHGNL
     QSCPTRSHAV WEMVMNELDR REDPVNDEYL PGCAMVDSCS NILTGDQFYN FLNHNFDRHY
     DQNRAPLGLY FHAAWLKNNP EFLDAFLYWI DEILANHNDV YFVTMTQVIQ WMQNPRTISE
     VKNFEPWREK CVVEGKPACW VPNTCKLTSK EVPGETINLQ TCVRCPNNYP WVSDPTGDGF
     F
//
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