ID G1PXR5_MYOLU Unreviewed; 354 AA.
AC G1PXR5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=DNA damage inducible 1 homolog 2 {ECO:0000313|Ensembl:ENSMLUP00000016247.1};
GN Name=DDI2 {ECO:0000313|Ensembl:ENSMLUP00000016247.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000016247.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000016247.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000016247.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAPE02050543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PXR5; -.
DR STRING; 59463.ENSMLUP00000016247; -.
DR Ensembl; ENSMLUT00000022970.1; ENSMLUP00000016247.1; ENSMLUG00000030669.1.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_020435_1_0_1; -.
DR InParanoid; G1PXR5; -.
DR OMA; QIGNDHL; -.
DR TreeFam; TF333421; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IEA:Ensembl.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0097752; P:regulation of DNA stability; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR CDD; cd05479; RP_DDI; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15397:SF3; DNA DAMAGE-INDUCIBLE 1 HOMOLOG 2; 1.
DR PANTHER; PTHR15397; SODIUM-GLUCOSE COTRANSPORTER REGULATORY PROTEIN -RELATED; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 165..288
FT /note="Aspartic peptidase DDI1-type"
FT /evidence="ECO:0000259|Pfam:PF09668"
FT REGION 32..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 39277 MW; 7F38F0B5CB645AAD CRC64;
IVHAERPLTD NHRSLASYGL KDGDVVILRQ KENVDPRPSQ FPNLPRIDFR SISVPGTSSS
RQRQPPGAQQ SHSSPGELAL SPQGLDNPAL LRDMLLANPH ELSLLKERNP PLADALLSGD
LEKFTRVLVE QQQDRARREQ ERIRLFSADP FDLEAQAKIE EDIRQQNIEE NMTIAMEEAP
ESFGQVVMLY INCKVNGHPV KAFVDSGAQM TIMSQACAER CNIMRLVDRR WAGIAKGVGT
QKIIGRVHLA QVQIEGDFLA CSFSILEEQP MDMLLGLDML KRHQCSIDLK KNVLVIGTTG
SQTTFLPEAE LPECARLAYG AGREEVLRPE EIADRELAEA LQKSVQDAGI CSAG
//
