ACD_RAT
ID ACD_RAT Reviewed; 417 AA.
AC Q4FZR5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Adrenocortical dysplasia protein homolog {ECO:0000305};
GN Name=Acd {ECO:0000312|RGD:1565053};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the shelterin complex (telosome) that is
CC involved in the regulation of telomere length and protection. Shelterin
CC associates with arrays of double-stranded TTAGGG repeats added by
CC telomerase and protects chromosome ends. Without its protective
CC activity, telomeres are no longer hidden from the DNA damage
CC surveillance and chromosome ends are inappropriately processed by DNA
CC repair pathways. Promotes binding of POT1 to single-stranded telomeric
CC DNA. Modulates the inhibitory effects of POT1 on telomere elongation.
CC The ACD-POT1 heterodimer enhances telomere elongation by recruiting
CC telomerase to telomeres and increasing its processivity. May play a
CC role in organogenesis. {ECO:0000250|UniProtKB:Q96AP0}.
CC -!- SUBUNIT: Component of the shelterin complex (telosome) composed of
CC TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Forms heterodimers with
CC POT1. Identified in a complex with POT1 and single-stranded telomeric
CC DNA. Interacts with STN1 and TINF2. {ECO:0000250|UniProtKB:Q96AP0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96AP0}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q96AP0}.
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DR EMBL; BC099222; AAH99222.1; -; mRNA.
DR RefSeq; NP_001032270.1; NM_001037193.1.
DR AlphaFoldDB; Q4FZR5; -.
DR SMR; Q4FZR5; -.
DR STRING; 10116.ENSRNOP00000056334; -.
DR iPTMnet; Q4FZR5; -.
DR PhosphoSitePlus; Q4FZR5; -.
DR PaxDb; Q4FZR5; -.
DR GeneID; 307798; -.
DR KEGG; rno:307798; -.
DR UCSC; RGD:1565053; rat.
DR CTD; 65057; -.
DR RGD; 1565053; Acd.
DR VEuPathDB; HostDB:ENSRNOG00000038973; -.
DR eggNOG; ENOG502SAN8; Eukaryota.
DR HOGENOM; CLU_619569_0_0_1; -.
DR InParanoid; Q4FZR5; -.
DR OMA; YEPPCAS; -.
DR OrthoDB; 841353at2759; -.
DR PhylomeDB; Q4FZR5; -.
DR TreeFam; TF338536; -.
DR Reactome; R-RNO-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-RNO-110331; Cleavage of the damaged purine.
DR Reactome; R-RNO-171306; Packaging Of Telomere Ends.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR Reactome; R-RNO-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-RNO-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-RNO-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-RNO-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-RNO-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-9670095; Inhibition of DNA recombination at telomere.
DR PRO; PR:Q4FZR5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000038973; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q4FZR5; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0000783; C:nuclear telomere cap complex; ISO:RGD.
DR GO; GO:0070187; C:shelterin complex; ISO:RGD.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IEA:InterPro.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0060381; P:positive regulation of single-stranded telomeric DNA binding; ISO:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; ISO:RGD.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:RGD.
DR GO; GO:0035282; P:segmentation; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0032202; P:telomere assembly; ISO:RGD.
DR GO; GO:0016233; P:telomere capping; ISO:RGD.
DR GO; GO:0000723; P:telomere maintenance; ISO:RGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IEA:InterPro.
DR GO; GO:0001655; P:urogenital system development; ISO:RGD.
DR InterPro; IPR028631; ACD.
DR InterPro; IPR019437; TPP1/Est3.
DR PANTHER; PTHR14487; PTHR14487; 1.
DR Pfam; PF10341; TPP1; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere; Ubl conjugation.
FT CHAIN 1..417
FT /note="Adrenocortical dysplasia protein homolog"
FT /id="PRO_0000239021"
FT REGION 156..245
FT /note="Interaction with POT1"
FT /evidence="ECO:0000250"
FT REGION 237..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..13
FT /note="PWI"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EE38"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AP0"
FT CROSSLNK 348
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AP0"
SQ SEQUENCE 417 AA; 45591 MW; 0D71769328AEF1B7 CRC64;
MSNSGRLVLR PWIRELILGS ETLSSPQAGH LLKVLQDSET PGPSSAPDTP DTGAVLLVSD
GTHSVRCVVT RNAIDTSDWE EKEFGFRGTE GRLLLLQACG LRIQVAQDYA PAEFYLQVDR
FNLLPTEQPR VQVTGCNQDS DVQKKLNKCL EDHLSESASS SAGLTLSQLL DEVKEDGDHR
GALVRLAESC LVLQGPFTAR PLTHWATSCS QATEEAVFTV PSFLLHISEN EEQILSSIDS
SQKAQENPAS PSLMPQEESG ASVSLLSALP TSDPGQKDNS QPPPTVCSTS PRAQAPSSTP
CSSTPSSPLL TCSPSLSPLR HAPTSYQACE TRTQFHKLEF RELQWPIKRR QLLPRTGAQE
PHSVWEPPER HRDTSAFQYK YGTPSASLHT QVQTARLSPQ LVAWALNIVM ESELPQV
