GenomeNet

Database: UniProt
Entry: G3P3X7_GASAC
LinkDB: G3P3X7_GASAC
Original site: G3P3X7_GASAC 
ID   G3P3X7_GASAC            Unreviewed;       497 AA.
AC   G3P3X7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   10-JUN-2026, entry version 67.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000012300.1};
OS   Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000012300.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000012300.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000012300.1,
RC   ECO:0000313|Proteomes:UP000007635};
RX   PubMed=33598708;
RA   Nath S., Shaw D.E., White M.A.;
RT   "Improved contiguity of the threespine stickleback genome using long-read
RT   sequencing.";
RL   G3 (Bethesda) 11:0-0(2021).
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000012300.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
CC   -!- SIMILARITY: Belongs to the translokin family.
CC       {ECO:0000256|ARBA:ARBA00008179}.
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DR   RefSeq; XP_040054899.1; XM_040198965.1.
DR   AlphaFoldDB; G3P3X7; -.
DR   STRING; 69293.ENSGACP00000012300; -.
DR   Ensembl; ENSGACT00000012324.2; ENSGACP00000012300.1; ENSGACG00000009314.2.
DR   eggNOG; ENOG502QTZR; Eukaryota.
DR   GeneTree; ENSGT00530000063695; -.
DR   InParanoid; G3P3X7; -.
DR   OMA; TQNNAEM; -.
DR   Proteomes; UP000007635; Chromosome I.
DR   Bgee; ENSGACG00000009314; Expressed in embryo and 4 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   Gene3D; 1.20.58.90; -; 1.
DR   InterPro; IPR051756; Centrosomal_MT-associated.
DR   InterPro; IPR025913; Cep57_CLD.
DR   InterPro; IPR024957; Cep57_MT-bd_dom.
DR   PANTHER; PTHR19336:SF11; CENTROSOMAL PROTEIN OF 57 KDA; 1.
DR   PANTHER; PTHR19336; UNCHARACTERIZED DUF1167; 1.
DR   Pfam; PF14073; Cep57_CLD; 1.
DR   Pfam; PF06657; Cep57_MT_bd; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT   DOMAIN          77..264
FT                   /note="Cep57 centrosome localisation"
FT                   /evidence="ECO:0000259|Pfam:PF14073"
FT   DOMAIN          361..433
FT                   /note="Cep57 centrosome microtubule-binding"
FT                   /evidence="ECO:0000259|Pfam:PF06657"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..101
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          148..182
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          208..249
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          376..426
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        8..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..60
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..371
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  56165 MW;  B5F0F8DED5C29934 CRC64;
     METLSKTADA DATREREPPA PRGVVSDSFS LPSYKDYPPH RPFINTLLHH TPKTRSHQPR
     RSSSPGNAFP ETSSAEILSA LRNLQEKIMR LELEKGHAER GLHAVGQNVP YAPLQREEVA
     QRLSGDHGEP EREISGESNN NQVLITHLAA AESRCLKLER QLDHMRRMLR SAKAERSSLL
     RQQVSMETAR SAEKQPDTVC EQAQLETLER LEQEYLRLTH TQNNAEMKMR QLEIKLLEEE
     HQRKLVQDKA NQLQTGLETN RILLQSVSPC LSSRPSKEKK SYSKKSSPQH SSCTQPHYRL
     SLRDVPFVAG TSVGCSHSVR ANVQSVLSLL KRHQPHLCNR RVLSSDANGH ETGCRRPSDA
     SSSSASASGG ELSELLQALE EELRLMSLER DELTGQVEAS VTDQERKELQ REQERLLQKM
     ERKGEQINKL HKHRTHIKKL RKEANSRRSC GSERRVASTT SARGRCPAPV KVGPGERSKG
     NLRLLRDMRA LQTSLRT
//
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