ID A0A3Q2ZMJ8_KRYMA Unreviewed; 512 AA.
AC A0A3Q2ZMJ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSKMAP00000004205.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000004205.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000004205.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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 AlphaFoldDB; A0A3Q2ZMJ8; -.
DR Ensembl; ENSKMAT00000004288.1; ENSKMAP00000004205.1; ENSKMAG00000003134.1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR033929; Tensin_PTB.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 253..362
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 60..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 55343 MW; 7E5A1676DF929664 CRC64;
LTKTPLSALG LKPQQGGSGQ SLQICLLTAE DVQNLSKYET IFNSASENQR GFVCFGVRRR
TGSSDSAPHR PASPEGSQVD IMGVHTVPGS PNTLHRTVAT NTPPSPALQR RLGQGSPSLA
RHPFPTGVPT SPLIGRNPKM AAAGMPPSPL MGRRAPSSGH STPDELGAAS RQGSAQPPPT
PAFPVSPQLP EKRHMSSGDA ERTDNRNLTP VSGGSTPNLS GTHPLPDASK SIYDSYPDIK
MNVKFVQDTS KFWYKPDISR EQAISLLKDR EPGAFIIRDS HSFRGAYGLA MKVACPPPTI
QQNKKAGDMT NELVRHFLIE TSSKGVRLKG CPNEPYFGCL SALVYQHSMT PLALPCKLMI
PTKDVPLLCF HTLLFYCLFP ACNVLYINSV DMESLTGPQA VAKAISQTLA TNPLPAATTV
HFKVSAQGIT LTDSQRKIFF RRHYPINTVT YCDMDPQNRK WGKEGGGSVK LFGFVARKQG
STTDNVSHLF AELDPDQPAS AIVSFVSKTM KQ
//