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Protein

Adrenocortical dysplasia protein

Gene

Acd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodimer enhances telomere elongation by recruiting telomerase to telomeres and increasing its processivity (By similarity). May play a role in organogenesis (PubMed:15537664).By similarity1 Publication

GO - Molecular functioni

  • DNA polymerase binding Source: MGI
  • macromolecular complex binding Source: MGI
  • telomeric DNA binding Source: BHF-UCL

GO - Biological processi

  • embryonic limb morphogenesis Source: MGI
  • establishment of protein localization to telomere Source: MGI
  • intracellular protein transport Source: MGI
  • negative regulation of telomere maintenance via telomerase Source: MGI
  • positive regulation of single-stranded telomeric DNA binding Source: MGI
  • positive regulation of telomerase activity Source: MGI
  • positive regulation of telomere maintenance via telomerase Source: MGI
  • protection from non-homologous end joining at telomere Source: BHF-UCL
  • protein localization to chromosome, telomeric region Source: MGI
  • segmentation Source: MGI
  • skeletal system development Source: MGI
  • telomere assembly Source: MGI
  • telomere capping Source: BHF-UCL
  • telomere maintenance Source: MGI
  • urogenital system development Source: MGI
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Adrenocortical dysplasia protein
Gene namesi
Name:Acd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:87873. Acd.

Subcellular locationi

  • Nucleus By similarity
  • Chromosometelomere By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear telomere cap complex Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • telosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Defects in Acd are the cause of adrenocortical dysplasia (ACD). ACD is a spontaneous autosomal recessive mouse mutant resulting from spontaneous splicing mutation of acd. ACD mice are characterized by developmental defects in organs derived from the urogenital ridge, reduced survival, poor growth, skin hyperpigmentation and adrenal insufficiency. Forty percent of the mutants died within 24 hours. Analysis of E14.5 to E17.5 embryos revealed reduced formation of caudal structure as well as limb defects.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Adrenocortical dysplasia proteinPRO_0000239020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei313 – 3131PhosphoserineCombined sources
Modified residuei317 – 3171PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5EE38.
MaxQBiQ5EE38.
PaxDbiQ5EE38.
PRIDEiQ5EE38.

PTM databases

iPTMnetiQ5EE38.
PhosphoSiteiQ5EE38.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

Expressed from E7 to E18 throughout development.1 Publication

Gene expression databases

BgeeiQ5EE38.
CleanExiMM_ACD.
ExpressionAtlasiQ5EE38. baseline and differential.
GenevisibleiQ5EE38. MM.

Interactioni

Subunit structurei

Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Forms heterodimers with POT1. Identified in a complex with POT1 and single-stranded telomeric DNA. Interacts with STN1/OBFC1 and TINF2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Obfc1Q8K2X32EBI-6258642,EBI-2553883

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-29612N.
IntActiQ5EE38. 7 interactions.
STRINGi10090.ENSMUSP00000048180.

Structurei

3D structure databases

ProteinModelPortaliQ5EE38.
SMRiQ5EE38. Positions 4-153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 24590Interaction with POT1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 133PWI

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi236 – 31782Ser-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IGMZ. Eukaryota.
ENOG410YTBM. LUCA.
GeneTreeiENSGT00390000004877.
HOGENOMiHOG000033778.
HOVERGENiHBG080817.
InParanoidiQ5EE38.
KOiK11114.
OMAiWEEKEFG.
OrthoDBiEOG7HHWSJ.
PhylomeDBiQ5EE38.
TreeFamiTF338536.

Family and domain databases

InterProiIPR028631. ACD.
[Graphical view]
PANTHERiPTHR14487. PTHR14487. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5EE38-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDSGLLALQ PWIRELILGS ETLSSPRTGQ LLKVLQDSET PGPSSAPDTP
60 70 80 90 100
DTGAVLLVSD GTHSVRCVVT RNAIDTSDWE EKELGFRGTE GRLLLLQACG
110 120 130 140 150
LRVQVAQDHA PAEFYLQVDR FNLLPTEQPR IQVTGCNQDS DVQRKLNECL
160 170 180 190 200
EDHLSESASS SAGLTLSQLL DEVREDQDHR GALVCLAKSC LVLKGPCTTT
210 220 230 240 250
PLTDWITSGS QALGKAVFTV SGSLLHIPEG EEQILSSTGS SQKARGTSAS
260 270 280 290 300
PSHMPLEESG ASVSLLSALA TSDPGQMDSS QSPPAVGSTS PRAQAPTSPP
310 320 330 340 350
CNSTPSSLLL NCSPSLSPLH PAPRSHQSCE TRAQAPKLEF QCSFKKRQLL
360 370 380 390 400
PRTSAQELCS VWEPPERHRD TSAFQYKYET PSASLHTQVQ TARLSPQLVA
410
WALNIVMESE SELTQV
Length:416
Mass (Da):44,713
Last modified:March 15, 2005 - v1
Checksum:i357CB31A8C4639BF
GO
Isoform 2 (identifier: Q5EE38-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     101-136: LRVQVAQDHAPAEFYLQVDRFNLLPTEQPRIQVTGC → MKLPPFVSSRALGIDLQVRGMGINNPDHLPPSSSPS

Note: No experimental confirmation available.
Show »
Length:316
Mass (Da):33,731
Checksum:iA46478B40D1752B6
GO
Isoform 3 (identifier: Q5EE38-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-191: Missing.
     192-213: VLKGPCTTTPLTDWITSGSQAL → MCRENSMSVLRTTSQSLLLPVQ

Note: No experimental confirmation available.
Show »
Length:225
Mass (Da):24,126
Checksum:i693277F805084F65
GO
Isoform 4 (identifier: Q5EE38-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-253: Missing.

Note: No experimental confirmation available.
Show »
Length:163
Mass (Da):17,629
Checksum:iE8BFEC040F32A3A5
GO
Isoform 5 (identifier: Q5EE38-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.
     159-162: SSSA → MLAP
     214-232: GKAVFTVSGSLLHIPEGEE → VSAGLFLGGFRGRVRQLPC
     233-416: Missing.

Note: No experimental confirmation available.
Show »
Length:74
Mass (Da):7,883
Checksum:iF74862718297BF4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581A → T in BAE35904 (PubMed:16141072).Curated
Sequence conflicti393 – 3931R → W in BAE20450 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 253253Missing in isoform 4. 1 PublicationVSP_019067Add
BLAST
Alternative sequencei1 – 191191Missing in isoform 3. 1 PublicationVSP_019068Add
BLAST
Alternative sequencei1 – 158158Missing in isoform 5. 1 PublicationVSP_019069Add
BLAST
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_019070Add
BLAST
Alternative sequencei101 – 13636LRVQV…QVTGC → MKLPPFVSSRALGIDLQVRG MGINNPDHLPPSSSPS in isoform 2. 1 PublicationVSP_019071Add
BLAST
Alternative sequencei159 – 1624SSSA → MLAP in isoform 5. 1 PublicationVSP_019072
Alternative sequencei192 – 21322VLKGP…GSQAL → MCRENSMSVLRTTSQSLLLP VQ in isoform 3. 1 PublicationVSP_019073Add
BLAST
Alternative sequencei214 – 23219GKAVF…PEGEE → VSAGLFLGGFRGRVRQLPC in isoform 5. 1 PublicationVSP_019074Add
BLAST
Alternative sequencei233 – 416184Missing in isoform 5. 1 PublicationVSP_019075Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY902197 Genomic DNA. Translation: AAW82804.1.
AK030405 mRNA. Translation: BAE20450.1.
AK032683 mRNA. Translation: BAE43282.1.
AK145959 mRNA. Translation: BAE26785.1.
AK160599 mRNA. Translation: BAE35904.1.
AK171345 mRNA. Translation: BAE42403.1.
BC004682 mRNA. Translation: AAH04682.1.
CCDSiCCDS22608.1. [Q5EE38-1]
RefSeqiNP_001012656.1. NM_001012638.1. [Q5EE38-1]
XP_006531237.1. XM_006531174.2. [Q5EE38-3]
XP_006531238.1. XM_006531175.1. [Q5EE38-3]
XP_006531239.1. XM_006531176.1. [Q5EE38-3]
XP_011246737.1. XM_011248435.1. [Q5EE38-3]
UniGeneiMm.12964.

Genome annotation databases

EnsembliENSMUST00000042608; ENSMUSP00000048180; ENSMUSG00000038000. [Q5EE38-1]
GeneIDi497652.
KEGGimmu:497652.
UCSCiuc009ndq.1. mouse. [Q5EE38-1]
uc009ndr.1. mouse. [Q5EE38-4]
uc009ndt.1. mouse. [Q5EE38-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY902197 Genomic DNA. Translation: AAW82804.1.
AK030405 mRNA. Translation: BAE20450.1.
AK032683 mRNA. Translation: BAE43282.1.
AK145959 mRNA. Translation: BAE26785.1.
AK160599 mRNA. Translation: BAE35904.1.
AK171345 mRNA. Translation: BAE42403.1.
BC004682 mRNA. Translation: AAH04682.1.
CCDSiCCDS22608.1. [Q5EE38-1]
RefSeqiNP_001012656.1. NM_001012638.1. [Q5EE38-1]
XP_006531237.1. XM_006531174.2. [Q5EE38-3]
XP_006531238.1. XM_006531175.1. [Q5EE38-3]
XP_006531239.1. XM_006531176.1. [Q5EE38-3]
XP_011246737.1. XM_011248435.1. [Q5EE38-3]
UniGeneiMm.12964.

3D structure databases

ProteinModelPortaliQ5EE38.
SMRiQ5EE38. Positions 4-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29612N.
IntActiQ5EE38. 7 interactions.
STRINGi10090.ENSMUSP00000048180.

PTM databases

iPTMnetiQ5EE38.
PhosphoSiteiQ5EE38.

Proteomic databases

EPDiQ5EE38.
MaxQBiQ5EE38.
PaxDbiQ5EE38.
PRIDEiQ5EE38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042608; ENSMUSP00000048180; ENSMUSG00000038000. [Q5EE38-1]
GeneIDi497652.
KEGGimmu:497652.
UCSCiuc009ndq.1. mouse. [Q5EE38-1]
uc009ndr.1. mouse. [Q5EE38-4]
uc009ndt.1. mouse. [Q5EE38-3]

Organism-specific databases

CTDi65057.
MGIiMGI:87873. Acd.

Phylogenomic databases

eggNOGiENOG410IGMZ. Eukaryota.
ENOG410YTBM. LUCA.
GeneTreeiENSGT00390000004877.
HOGENOMiHOG000033778.
HOVERGENiHBG080817.
InParanoidiQ5EE38.
KOiK11114.
OMAiWEEKEFG.
OrthoDBiEOG7HHWSJ.
PhylomeDBiQ5EE38.
TreeFamiTF338536.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Miscellaneous databases

PROiQ5EE38.
SOURCEiSearch...

Gene expression databases

BgeeiQ5EE38.
CleanExiMM_ACD.
ExpressionAtlasiQ5EE38. baseline and differential.
GenevisibleiQ5EE38. MM.

Family and domain databases

InterProiIPR028631. ACD.
[Graphical view]
PANTHERiPTHR14487. PTHR14487. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Urogenital and caudal dysgenesis in adrenocortical dysplasia (acd) mice is caused by a splicing mutation in a novel telomeric regulator."
    Keegan C.E., Hutz J.E., Else T., Adamska M., Shah S.P., Kent A.E., Howes J.M., Beamer W.G., Hammer G.D.
    Hum. Mol. Genet. 14:113-123(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, FUNCTION, INVOLVEMENT IN ACD.
    Strain: DW/J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Adrenal gland, Cerebellum, Embryo, Pituitary and Placenta.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation."
    Wan M., Qin J., Songyang Z., Liu D.
    J. Biol. Chem. 284:26725-26731(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OBFC1.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-313 AND SER-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiACD_MOUSE
AccessioniPrimary (citable) accession number: Q5EE38
Secondary accession number(s): Q3TBB1
, Q3TUR7, Q3UKL6, Q3V3Y1, Q99KF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Adrenocortical dysplasia mouse was initially reported as a model of human congenital adrenal hypoplasia (AHC).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.