ID   TIRR_CHICK              Reviewed;         314 AA.
AC   Q9IAY5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tudor-interacting repair regulator protein {ECO:0000250|UniProtKB:Q9BRJ7};
DE   AltName: Full=NUDT16-like protein 1 {ECO:0000250|UniProtKB:Q9BRJ7};
DE   AltName: Full=Protein syndesmos {ECO:0000303|PubMed:10633082};
GN   Name=NUDT16L1; Synonyms=SDOS, TIRR {ECO:0000250|UniProtKB:Q9BRJ7};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   INTERACTION WITH SDC4, AND MYRISTOYLATION AT GLY-2.
RC   TISSUE=Embryo;
RX   PubMed=10633082; DOI=10.1242/jcs.113.2.315;
RA   Baciu P.C., Saoncella S., Lee S.H., Denhez F., Leuthardt D., Goetinck P.F.;
RT   "Syndesmos, a protein that interacts with the cytoplasmic domain of
RT   syndecan-4, mediates cell spreading and actin cytoskeletal organization.";
RL   J. Cell Sci. 113:315-324(2000).
CC   -!- FUNCTION: Key regulator of TP53BP1 required to stabilize TP53BP1 and
CC       regulate its recruitment to chromatin. {ECO:0000250|UniProtKB:Q9BRJ7}.
CC   -!- SUBUNIT: Interacts (via the cytoplasmic part) with syndecan-4 (SDC4),
CC       but not with other syndecan proteins (PubMed:10633082).
CC       {ECO:0000269|PubMed:10633082}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BRJ7}.
CC       Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10633082}. Cell membrane
CC       {ECO:0000305|PubMed:10633082}; Lipid-anchor
CC       {ECO:0000305|PubMed:10633082}; Cytoplasmic side {ECO:0000305}. Cell
CC       junction, focal adhesion {ECO:0000269|PubMed:10633082}.
CC       Note=Colocalizes with SDC4 in ventral plasma membrane adhesion plaques.
CC       {ECO:0000269|PubMed:10633082}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in embryonic
CC       brain, eyes, gizzard, heart, intestine, kidney, liver, tibia and skin.
CC       {ECO:0000269|PubMed:10633082}.
CC   -!- PTM: Myristoylated in vitro; additional evidence is however required to
CC       confirm myristoylation in vivo. {ECO:0000269|PubMed:10633082}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. TIRR subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to the nudix NUDT16 protein, lacks
CC       the Nudix box and is therefore not related to the rest of the family.
CC       Lacks a number of residues which are necessary for hydrolase activity
CC       and does not play a role in U8 snoRNA decapping activity.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF29566.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF095446; AAF29566.1; ALT_INIT; mRNA.
DR   RefSeq; NP_990111.1; NM_204780.1.
DR   AlphaFoldDB; Q9IAY5; -.
DR   SMR; Q9IAY5; -.
DR   BioGRID; 675838; 2.
DR   STRING; 9031.ENSGALP00000041772; -.
DR   iPTMnet; Q9IAY5; -.
DR   GeneID; 395557; -.
DR   KEGG; gga:395557; -.
DR   CTD; 84309; -.
DR   VEuPathDB; HostDB:geneid_395557; -.
DR   eggNOG; ENOG502S20E; Eukaryota.
DR   HOGENOM; CLU_075322_0_0_1; -.
DR   InParanoid; Q9IAY5; -.
DR   OrthoDB; 1385294at2759; -.
DR   PhylomeDB; Q9IAY5; -.
DR   PRO; PR:Q9IAY5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR   GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   SUPFAM; SSF55811; SSF55811; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein;
KW   Membrane; Myristate; Nucleus; Reference proteome; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..314
FT                   /note="Tudor-interacting repair regulator protein"
FT                   /id="PRO_0000097647"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000305|PubMed:10633082"
SQ   SEQUENCE   314 AA;  33296 MW;  8DC571DA242DA4BF CRC64;
     MGVMAAVGAL PAGAGSLPPL PTLGVPGVPE LKPLTRYEAM RLGPGWSHSC HAMLYAPNPG
     MLFGRIPLRY AVLMQMRFDG LLGFPGGFVD RRYWSLEDGL NRVLGLGLGC VRLTEADYLC
     SHLTDGPHRV VAHLYARQLT LEELHTIEIS AVHSRDHGLE VMGMVRVPLY TQKDRMGGLP
     NFLANSFVGT AKFQLLFALK ILNMVPEEKL AEAVAATQKP KKPAIDHAAV AAAKQANELA
     AAARAGNEYA DSGENQAAAH AAAELAEQQA AGLESQAVLE HLAAVPGAEA VVAELHAQPG
     ADAVLEQPVA EAME