ID A0A096M785_POEFO Unreviewed; 778 AA.
AC A0A096M785;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Tensin-like {ECO:0000313|Ensembl:ENSPFOP00000027276.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000027276.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000027276.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR EMBL; AYCK01011975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01011976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096M785; -.
DR Ensembl; ENSPFOT00000027012.1; ENSPFOP00000027276.1; ENSPFOG00000014114.2.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20888; C1_TNS1_v; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 19..66
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 128..300
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 305..431
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 86746 MW; 15690D9C1F192AF4 CRC64;
QQVCLIVFLQ PDELEGVHTH TFKLKPFKKA KSCDICKQAI TKEGLICKAC RLSCHKKCEV
KTATSCEPVE EDELQPEFSF SSTKNELDDQ SSATRNGNFN KLFNDDGSTR SCKSVEIRRK
QSGKDSVLQA MEESYEVDLV YITERIISLS FPAAADERSY TNNLKEVATM LQSKHGEHYL
VLNLSEQRND LTKLNHKVLE FGWPDHHAPA LDKICSMCKA MDTWLSGDQR NVVLLHNKGN
RGRTGVVVAA YMHYSNISAS ADQALDRFAM RRFYEDKALP GGQPSQRRYV QYFNGLLSGH
IKINNKPLFL HHVIMHGIPN FESKGGCRPF LKIYQAMQPV YTSGIYNVQG DSNTSICITI
EPGLLLKGDI LLKCYHKRYR NPTRDVVFRV QFHTCAIHDL GVVFGKAELD ETFKDERFPE
YGKVEFVFSY GPEKIRGLDH LENGPSVSVD YNTQDPLIRW DSYESFSHPS EDAVDTENDV
GHTQGPLDGS LYARVRKKDS LEQSNHHLQK TEQSLPVAGH TSLPAVDHTL SVSSDSGNST
ASIKTDRTDE HSHSLHTAAG HSNSTTAHPT LSPQEKRELD QLLSGLEPPT QRQAYLSTST
SPGGGVRHLV PAQVHVNGGH TRILRAPSTE ERETDILDDE LPNSQEGNSV DSLGTLSSLE
GQATPASLYY QSQTPVGGQN DGPYLERNVL GEKLNEMPVH GVQTPTAMQE RSVDSPSLQV
GYNNYQNGGG MYRSQSFGNQ PPSSPETNPK MMPKAPERST SSREAVQRGL NHWHQHSL
//
