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CAV_DROYA
ID   CAV_DROYA               Reviewed;         319 AA.
AC   B4PKZ7; B6UW57; O16047;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Telomere-binding protein cav {ECO:0000250|UniProtKB:Q95RV2};
DE   AltName: Full=Anon-EST:fe1G5 {ECO:0000312|EMBL:EDW98982.1};
GN   Name=cav {ECO:0000250|UniProtKB:Q95RV2};
GN   Synonyms=anon-EST:fe1G5 {ECO:0000312|EMBL:EDW98982.1}; ORFNames=GE23460;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:AAB81483.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9275195; DOI=10.1073/pnas.94.18.9746;
RA   Schmid K.J., Tautz D.;
RT   "A screen for fast evolving genes from Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9746-9750(1997).
RN   [2] {ECO:0000312|EMBL:EDW98982.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW98982.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [3] {ECO:0000312|EMBL:ACI96380.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141.
RX   PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA   Anderson J.A., Gilliland W.D., Langley C.H.;
RT   "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL   Genetics 181:177-185(2009).
CC   -!- FUNCTION: Binds to chromosome ends in a sequence-dependent manner and
CC       is required for telomere capping. {ECO:0000250|UniProtKB:Q95RV2}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with Su(var)205 dimer (via hinge
CC       and chromoshadow domain) and with moi to form the terminin, telomere-
CC       capping, complex. Interacts with HP6, which is also part of the
CC       terminin complex (By similarity). {ECO:0000250|UniProtKB:Q95RV2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q95RV2}.
CC       Chromosome, telomere {ECO:0000250|UniProtKB:Q95RV2}.
CC   -!- MISCELLANEOUS: Multiple telomeric associations (TAs) in the same
CC       metaphase spread often result in multicentric linear chromosomes that
CC       resemble little 'trains' of chromosomes, hence the name 'caravaggio',
CC       an Italian train.
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DR   EMBL; AF005852; AAB81483.1; -; mRNA.
DR   EMBL; CM000160; EDW98982.1; -; Genomic_DNA.
DR   EMBL; FJ218755; ACI96380.1; -; Genomic_DNA.
DR   RefSeq; XP_002099270.1; XM_002099234.2.
DR   AlphaFoldDB; B4PKZ7; -.
DR   STRING; 7245.FBpp0268470; -.
DR   EnsemblMetazoa; FBtr0269978; FBpp0268470; FBgn0022414.
DR   GeneID; 6538756; -.
DR   KEGG; dya:Dyak_GE23460; -.
DR   eggNOG; ENOG502RN8H; Eukaryota.
DR   HOGENOM; CLU_059636_0_0_1; -.
DR   OMA; QINSESM; -.
DR   OrthoDB; 1158010at2759; -.
DR   PhylomeDB; B4PKZ7; -.
DR   ChiTaRS; cav; fly.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000782; C:telomere cap complex; ISS:UniProtKB.
DR   GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR   GO; GO:0016233; P:telomere capping; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleus; Repeat; Telomere.
FT   CHAIN           1..319
FT                   /note="Telomere-binding protein cav"
FT                   /id="PRO_0000379492"
FT   REGION          107..312
FT                   /note="Required for binding to Su(var)205"
FT                   /evidence="ECO:0000250|UniProtKB:Q95RV2"
FT   REGION          141..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           220..224
FT                   /note="Su(var)205-binding Pro-containing repeat 1"
FT                   /evidence="ECO:0000255"
FT   MOTIF           273..279
FT                   /note="Su(var)205-binding Pro-containing repeat 2"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        233..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        81
FT                   /note="K -> R (in Ref. 1; AAB81483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="G -> A (in Ref. 1; AAB81483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="D -> E (in Ref. 1; AAB81483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="G -> A (in Ref. 1; AAB81483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="V -> ARDV (in Ref. 1; AAB81483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  36929 MW;  A013F8AB188D8D6B CRC64;
     MSGMQISSYL RKYLADEDKK IREEFKESDP NNEMILWMHE KTRITEEDLA RPYTEDEVRE
     LCLRTKVKVN MTAWNCLWEA KKRFDAKGRF ERKSEEFINL MYLKAVRRKM VQPYPEDYVA
     QRREIAAAET KKDNISRLDR WQKQKRRNQS AHATQPDSQD NEVVEIHDDT NRYSVSQAVA
     LPVLTPSDLS GIGDDEDEQQ QQHHHHKHRS GFQNEHADCP ETQMRCDQAD SGRLPNGPTN
     SESDPDYYMF GTQLSRSIQP TSTQEADDQL ACPETEMNES WVRCDQINSE SMSIGPSINS
     DGSISFQNSG SEPIDVDVN
 
 
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