ID A0A452HMT2_9SAUR Unreviewed; 923 AA.
AC A0A452HMT2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000016309.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000016309.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000016309.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000256|ARBA:ARBA00009475}.
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DR AlphaFoldDB; A0A452HMT2; -.
DR STRING; 38772.ENSGAGP00000016309; -.
DR Ensembl; ENSGAGT00000018615.1; ENSGAGP00000016309.1; ENSGAGG00000012225.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051172; P:negative regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd20599; CYCLIN_RB; 1.
DR Gene3D; 1.10.472.140; -; 1.
DR Gene3D; 6.10.140.1380; -; 1.
DR Gene3D; 6.10.250.530; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR015030; RB_C.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742:SF17; RETINOBLASTOMA-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR13742; RETINOBLASTOMA-ASSOCIATED PROTEIN RB -RELATED; 1.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR Pfam; PF08934; Rb_C; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SMART; SM01369; Rb_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 78..219
FT /note="Retinoblastoma-associated protein N-terminal"
FT /evidence="ECO:0000259|SMART:SM01367"
FT DOMAIN 365..567
FT /note="Retinoblastoma-associated protein A-box"
FT /evidence="ECO:0000259|SMART:SM01368"
FT DOMAIN 654..741
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 762..922
FT /note="Retinoblastoma-associated protein C-terminal"
FT /evidence="ECO:0000259|SMART:SM01369"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 104692 MW; 7346F1CA77A23A46 CRC64;
MPPKPPRKGG AAAKGQRASP DRGTGGTSPP AAARLEFGET DFVALCDTLR VSDTVRANAW
KTYEKVSSAD GTLVGYSEKK KDMWGICIFI AAVDLDEMTF TFTELLKSIG MRVCTCFQLL
REMDVNMDTI STKVDSNVSR LNKKYDVLSA LYHKFERTCA LIYMIQASSQ TSAELSLPLV
LKTSWITFLL AKGKVLQMED DLVISFQLLL CVLDYFIKLS PPSMLKEPYK SHVSAMSVNG
STRAPRRGQS RSTRTSKQTD TDTKVIEVLC KEYGCNLDEV KNVYFTSFIP FLNSVGIVTS
NGLPEVEDLS KQYEELYLKN KDIDARLFLD NDETLQHNHI ECLQLERTPR KNNPDEELNL
ILPQTPVRAA MNTIQQLMMI LNSASDKPSD NLLSYFNNCT VNPKEGILAR VENLGNIFKE
KFAEAVGQGC AEIGSQRYKL GVRLYYRVME SMLKSEEERL SVHNFSKLLN NNIFHTSLLA
CAVEVVMATY GRNASQSDGT STETDLSFPW ILNVLDLKAF DFYKVIESFI KAEPSLTREM
IKHLERCEHR IMESLAWQSD SSLFDLIKQS KEREGQVDQP EPTCTFNFPL QHNHTAADLY
LSPVRSPKKK GSTASLNPTP IIDAQPVLAP QTQKPQKSTS LSLFYKKVYR LAYLRLNTLC
LRLLFDHPEL EHLIWTLFQH TLQNEYELMK DRHLDQIMMC SMYGICKVKN VDLRFKIIVT
AYKELTNTNQ ETFKRVLIRE GQYDSIIVFY NLVFMQKLKT NILQYASNRP PTLSPIPHIP
RSPYKFSNSP LRVPAGNNIY ISPLKSPYKF SEGMLSPTKM TPRSRILVSI GESFGTSEKF
QKINQMVGSS DHQLKRSAEV STAPKPLKRL RFDIEGQDEA DGSKHLPGES KFQQKLAEMT
STRTRMQKQK LNDGTDASAT EEK
//
