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DJSHV_DROME
ID   DJSHV_DROME             Reviewed;         354 AA.
AC   Q9VPQ2;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=DnaJ homolog shv {ECO:0000305};
DE   AltName: Full=Protein shriveled {ECO:0000303|PubMed:27191715};
DE   Flags: Precursor;
GN   Name=shv {ECO:0000312|FlyBase:FBgn0031256};
GN   ORFNames=CG4164 {ECO:0000312|EMBL:AAF51493.1};
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:0000312|EMBL:AAK93202.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAK93202.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAK93202.1};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF LYS-253 AND ASP-255.
RX   PubMed=27191715; DOI=10.1371/journal.pgen.1006043;
RA   Lee J.Y., Chen J.Y., Shaw J.L., Chang K.T.;
RT   "Maintenance of stem cell niche integrity by a novel activator of integrin
RT   signaling.";
RL   PLoS Genet. 12:E1006043-E1006043(2016).
CC   -!- FUNCTION: Maintains stem cell niche architecture in the testes.
CC       Activates an extracellular integrin beta-PS pathway which regulates DE-
CC       cadherin (shg) levels in somatic hub cells, and is essential for
CC       maintaining the number of germline stem cells and the structure and
CC       localization of hub cells. {ECO:0000269|PubMed:27191715}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27191715}. Cell
CC       membrane {ECO:0000269|PubMed:27191715}. Secreted
CC       {ECO:0000269|PubMed:27191715}. Note=Secreted by somatic cells of the
CC       testes. Detected at the cell borders between the hub and germline stem
CC       cells, and between the germ and cyst stem cells.
CC       {ECO:0000269|PubMed:27191715}.
CC   -!- TISSUE SPECIFICITY: In the testes, detected at low levels in somatic
CC       hub cells, cyst stem cells and the apical tip (at protein level).
CC       Levels in the testes decrease with age (at protein level). Expressed at
CC       low levels in hub cells, cyst stem cells and germline stem cells, and
CC       at high levels in spermatocytes and cyst cells.
CC       {ECO:0000269|PubMed:27191715}.
CC   -!- DISRUPTION PHENOTYPE: Males are sterile and display an age-dependent
CC       decrease in testes size resulting from a gradual loss in somatic hub
CC       cell structure and a decrease in the number of germline stem cells. Hub
CC       cells frequently do not localize to the apical tip and are instead
CC       present throughout the testes. The number of hub cells is not affected.
CC       Reduced DE-cadherin levels in the hub cells. Absence of integrin
CC       clustering and decreased focal adhesion kinase (FAK) phosphorylation at
CC       the hub/cyst stem cell interface. {ECO:0000269|PubMed:27191715}.
CC   -!- MISCELLANEOUS: The name 'shriveled' derives from the shrinking testes
CC       phenotype of mutants. {ECO:0000303|PubMed:27191715}.
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DR   EMBL; AE014134; AAF51493.1; -; Genomic_DNA.
DR   EMBL; AY051778; AAK93202.1; -; mRNA.
DR   RefSeq; NP_608525.1; NM_134681.3.
DR   AlphaFoldDB; Q9VPQ2; -.
DR   SMR; Q9VPQ2; -.
DR   IntAct; Q9VPQ2; 3.
DR   STRING; 7227.FBpp0077720; -.
DR   GlyGen; Q9VPQ2; 2 sites.
DR   PaxDb; Q9VPQ2; -.
DR   PRIDE; Q9VPQ2; -.
DR   DNASU; 33220; -.
DR   EnsemblMetazoa; FBtr0078060; FBpp0077720; FBgn0031256.
DR   GeneID; 33220; -.
DR   KEGG; dme:Dmel_CG4164; -.
DR   UCSC; CG4164-RA; d. melanogaster.
DR   CTD; 33220; -.
DR   FlyBase; FBgn0031256; shv.
DR   VEuPathDB; VectorBase:FBgn0031256; -.
DR   eggNOG; KOG0713; Eukaryota.
DR   GeneTree; ENSGT00940000155792; -.
DR   HOGENOM; CLU_017633_0_0_1; -.
DR   InParanoid; Q9VPQ2; -.
DR   OMA; WDAGFEF; -.
DR   OrthoDB; 687505at2759; -.
DR   PhylomeDB; Q9VPQ2; -.
DR   SignaLink; Q9VPQ2; -.
DR   BioGRID-ORCS; 33220; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33220; -.
DR   PRO; PR:Q9VPQ2; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031256; Expressed in male reproductive gland and 32 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005178; F:integrin binding; IPI:FlyBase.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR   GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR   GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:FlyBase.
DR   GO; GO:0090129; P:positive regulation of synapse maturation; IMP:FlyBase.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Glycoprotein; Membrane; Nucleus;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..354
FT                   /note="DnaJ homolog shv"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5008180999"
FT   DOMAIN          25..90
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         253
FT                   /note="K->L: Loss of activity. Decrease in focal adhesion
FT                   kinase (FAK) phosphorylation and loss of cell spreading;
FT                   when associated with V-255."
FT                   /evidence="ECO:0000269|PubMed:27191715"
FT   MUTAGEN         255
FT                   /note="D->V: Loss of activity. Decrease in focal adhesion
FT                   kinase (FAK) phosphorylation and loss of cell spreading;
FT                   when associated with L-253."
FT                   /evidence="ECO:0000269|PubMed:27191715"
SQ   SEQUENCE   354 AA;  40212 MW;  880E4DC514D2C466 CRC64;
     MQLIKCLVII QLSLLLVEES FAGRDFYKIL NVKKNANTNE VKKAYRRLAK ELHPDKNKDD
     PDASTKFQDL GAAYEVLSNP DKRKTYDRCG EECLKKEGMM DHGGDPFSSF FGDFGFHFGG
     DGQQQDAPRG ADIVMDLYVS LEELYSGNFV EIVRNKPVTK PASGTRKCNC RQEMVTRNLG
     PGRFQMIQQT VCDECPNVKL VNEERTLEIE VEQGMVDGQE TRFVAEGEPH IDGEPGDLIV
     RVQQMPHPRF LRKNDDLYTN VTISLQDALV GFSMEIKHLD GHLVPVTREK VTWPGARIRK
     KGEGMPNFEN NNLTGNLYIT FDVEFPKKDL TEEDKEALKK ILDQSSINRI YNGL
 
 
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