ALMS1_DROME
ID ALMS1_DROME Reviewed; 1322 AA.
AC Q5BI31; Q9W4I8; Q9W4I9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Centrosome-associated protein Alms1a {ECO:0000305};
DE AltName: Full=Alstrom syndrome protein 1 homolog a {ECO:0000305};
GN Name=Alms1a {ECO:0000312|FlyBase:FBgn0025388};
GN Synonyms=EG:66A1.2 {ECO:0000312|FlyBase:FBgn0025388};
GN ORFNames=CG12179 {ECO:0000312|FlyBase:FBgn0025388};
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:AAX33541.1, ECO:0000312|EMBL:ACE82583.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAX33541.1, ECO:0000312|EMBL:ACE82583.1};
RA Booth B., Carlson J., Celniker S., Chavez C., Frise E., George R.,
RA Pacleb J., Park S., Rubin G.M., Wan K., Yu C., Stapleton M.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH KLP10A AND SAK, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32965218; DOI=10.7554/elife.59368;
RA Chen C., Yamashita Y.M.;
RT "Alstrom syndrome gene is a stem-cell-specific regulator of centriole
RT duplication in the Drosophila testis.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: In asymmetrically dividing germline stem cells (GSCs), plays
CC a critical role in ensuring centrosome duplication, which is essential
CC for the production of centrosomes and centrioles in all downstream germ
CC cells (PubMed:32965218). Might recruit SAK for daughter centriole
CC duplication (PubMed:32965218). {ECO:0000269|PubMed:32965218}.
CC -!- SUBUNIT: Interacts (via C-terminus) with Klp10A (PubMed:32965218).
CC Interacts with SAK (PubMed:32965218). {ECO:0000269|PubMed:32965218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:32965218}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:32965218}. Note=In male germline stem cells,
CC gonialblasts and spermatogonia, localizes to the proximal end of the
CC mother centrioles (PubMed:32965218). Only in male germ stem cells
CC (GSCs), localizes asymmetrically to the mother centrosomes and within
CC it with higher levels at both mother and daughter centrioles
CC (PubMed:32965218). Colocalizes with SAK at the mother centrosome in
CC GSCs (PubMed:32965218). {ECO:0000269|PubMed:32965218}.
CC -!- TISSUE SPECIFICITY: Expressed in all germlines, including germline stem
CC cells and spermatogonia. {ECO:0000269|PubMed:32965218}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in asymmetrically
CC dividing male germline stem cells (GSCs), results in loss of centriole
CC duplication and thereby leads to complete loss of centrosomes (and
CC centrioles) from all male germ cells (PubMed:32965218). In GSCs,
CC results in the enrichment of both SAK and Sas-6 at the remaining
CC elongated mother centrioles (PubMed:32965218). Does not change Klp10A
CC centrosome localization in male germline stem cells (PubMed:32965218).
CC RNAi-mediated knockdown in symmetrically dividing spermatogonia, does
CC not affect normal centrosome duplication (PubMed:32965218).
CC {ECO:0000269|PubMed:32965218}.
CC -!- SIMILARITY: Belongs to the ALMS1 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF45962.4; -; Genomic_DNA.
DR EMBL; AE014298; AAF45963.4; -; Genomic_DNA.
DR EMBL; BT021393; AAX33541.1; -; mRNA.
DR EMBL; BT033060; ACE82583.1; -; mRNA.
DR RefSeq; NP_572175.3; NM_131947.4.
DR RefSeq; NP_726937.3; NM_167011.4.
DR AlphaFoldDB; Q5BI31; -.
DR SMR; Q5BI31; -.
DR IntAct; Q5BI31; 5.
DR PaxDb; Q5BI31; -.
DR EnsemblMetazoa; FBtr0300754; FBpp0289978; FBgn0025388.
DR EnsemblMetazoa; FBtr0300755; FBpp0289979; FBgn0025388.
DR GeneID; 31393; -.
DR KEGG; dme:Dmel_CG12179; -.
DR UCSC; CG12179-RA; d. melanogaster.
DR UCSC; CG12179-RB; d. melanogaster.
DR FlyBase; FBgn0025388; Alms1a.
DR VEuPathDB; VectorBase:FBgn0025388; -.
DR eggNOG; ENOG502SFA4; Eukaryota.
DR GeneTree; ENSGT00540000073831; -.
DR HOGENOM; CLU_009110_0_0_1; -.
DR InParanoid; Q5BI31; -.
DR OMA; VNTCETT; -.
DR OrthoDB; 1100624at2759; -.
DR PhylomeDB; Q5BI31; -.
DR BioGRID-ORCS; 31393; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG12179; fly.
DR GenomeRNAi; 31393; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0025388; Expressed in cleaving embryo and 24 other tissues.
DR ExpressionAtlas; Q5BI31; baseline and differential.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:FlyBase.
DR GO; GO:0019894; F:kinesin binding; IPI:FlyBase.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0046601; P:positive regulation of centriole replication; IGI:FlyBase.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:FlyBase.
DR InterPro; IPR029299; ALMS_motif.
DR Pfam; PF15309; ALMS_motif; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1322
FT /note="Centrosome-associated protein Alms1a"
FT /evidence="ECO:0000305"
FT /id="PRO_0000451954"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1322
FT /note="Interaction with Klp10A"
FT /evidence="ECO:0000269|PubMed:32965218"
FT REGION 1190..1309
FT /note="ALMS motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 81..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..909
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 148123 MW; 2A10167AE179209D CRC64;
MRAKRGAVGK VMMSGSRHNK LAESSRVPPL AREYISAMAT DRELDRFMAL SSTASSGASG
STHSCALGSV PPPGCASMEH ESRPESGHRR RTKSSDHRSP DERGEAKEQL RELSVSPPPS
KHKISQFTSP KSEVTKTKPN EYTIIPIVLA SSPSFRSVAV TQTMSQSAED IRTPTKSPQM
QNKKTQTPES VLKSHKRLEW DPSADVGYCK RAMSMSNIST LERSVLEDCS WRQPTQQRPE
ANLDGVQPLL AEEPSPMLDK PTPPLACSTF VNRSERTKSL NSGMESSLSS NKGDPRKKCQ
RKSRRQDSEV SSCQTDCRSS SQKESTQGSS EAKDIRGNFT TEGTQCSYNR NDTEIDSIME
EEESIDRRKK DDLRISSRVQ DPQISSRRPS VSSSRRESLS SYRRDDSRLN SPNSSRLGSE
VSSRVESSRS SSRRESQTNS VYGSLSASSF DYHMHMAQEV EVLKHNQRRQ QEMEVEPKKQ
LEKEQHQNDM QQGEPKGREL KDKNHHSGRE QQEIQPLMRD QRKAEQRHEK DHQLEREQQG
IQQLSKGQRK AKKREKEREQ ERQYTAAQFE KIRSNRRHVN KENQKPENPV VNPSTGVTAS
TSTTSLDVGS GSRPGGELDL GIDLLCSLVK SRSLSQGQKK KLVRDIARRI SCLELTESST
SSRSLSSSSK EQLKVPTGSL QQVAATNTNQ SNARSSSKAE RIAPPVPAPR KRAAIGSSSP
LPESVSYSGS TSGSGEVITQ KTNIPNRNAS TDADIEPLDL QDWLNPMTLS EIEFEERLKG
GTDSERRRQL HWVKTEINRM QEFKNLLENI SLPSKSQKKA NTESATAAQI PSSMRCMGDQ
KERPDKEYLL RQEMSAEAES KEMENSETTT TPPPPVRIES VGVNVTNSDP STLPAPPPTQ
PPPPPPHLNQ RNLQNRKKMA TPLLVSGSST SGGGRSESVC SFVQQRQRQF REHYQNQQQQ
QFVLLQQQKL YQLQKQLNQQ KDILIQRQQH CGQCAQCGHQ RTCIHQQNCP RRQQEAEEQP
DEREQYMQMQ YAQAAGSAYA TPHQSGSSGA DKNEAIYYQV VNSQGVASYV QATMVSTETQ
NEASATGGAG GSAITRSTTT TTNSSSSMMC ISSDMSVPMG MMNTCETTTT TTTHQYDDVA
CQRVRRGHKE TTMNAESMQR QTLQVRPRAI SYVIQFTPTG SSEVIEKPPS LQDQLQLARP
EFCANAKQRK AILNEMQMIR NARRQELDNV LSQSTSMEAL NRHLEQLPPP ANTRVRLFTT
REMKAITSKR CKNLPEVLAA QSRQEEEQRR RSNRLMRDVF NKRLKSRVAS GQISLNHSMA
IM
