ID A0A3P8PEK2_ASTCA Unreviewed; 1692 AA.
AC A0A3P8PEK2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tensin-2-like {ECO:0000313|Ensembl:ENSACLP00000015419.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000015419.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000015419.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000015419.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSACLT00000015781.1; ENSACLP00000015419.1; ENSACLG00000010429.1.
DR GeneTree; ENSGT00940000163886; -.
DR Proteomes; UP000265100; Chromosome 20.
DR Bgee; ENSACLG00000010429; Expressed in liver and 8 other cell types or tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20887; C1_TNS2; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14562; PTP_tensin-2; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF1; TENSIN-2; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 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 SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 48..95
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 129..301
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 306..432
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1420..1543
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 496..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1692 AA; 187240 MW; 355B81342D1CA3C9 CRC64;
MGCVLSSDWC GEEEVQPVPV VRNSSLKRSL ERSESGRMRL TKAGKGEPHV FKEKTFKKKR
QCSVCRQSVD NVGSFCRVCK TATHRKCEAK VTFACTPAPS NDLGSTKSLT YTKQRNTLPR
SFSVDRVMER VMERNYDFDL TYITERIISV FFPPKLEEQR YRLNLKEVAA MLKSKHQEKF
LLLNLSERRH DITRLNPKVH DFGWPDLHAP PLDKICAICK AMENWLNSDP QHVVVLHCKG
NKGKTGVIIA AYMHYSKISA GADQALSTLA MRKFCEDKVS SSLQPSQNRY IYYFGGLLSG
AIKMNSSPLF LHQVLIPSLP NFQGEGGYYP FLKIYQSMQL VYTSGIYDLQ GTGGRRLCVT
IEPALLLKGD IMVKCYHRRA QSADRDTVFR LQFHTCTIHG SQLWFGKGEL DEACTDERFP
SDATVEFVFS SGPERIKGRE YHKNDPAVTV DYNTADPVVR WDSYENFNQR YQDSLEDIAH
TRGPLDGSLY AQIKKRRGPG SGSLTSANGS IAGGVAAEDR PDHRITQGSD SGLSAHSLHL
NQSSIHPDHQ EESNRPPPPT RQEREELERL LGGIEGSRDG ERETAILDDG DSIQSERTGT
LRLSRSCSCR DGYRSQRCAE PGCDRTLLMP NGYCLDRAPG TNGHHGAPPS ASPNPAAPPS
HMDLCQHYSP HSHQSLPPPD LVWDRQSGSP HYLHRSCSEA PSSRHTCPYP SADLTPHAHN
HPHHHPMSAP GRLCYREDEY TPYHHPPPPH SHHHPHQHQK PATSPTYHDI MLMDGLPPSG
CPCRDCSMRR EDSVAYHTLR MERGDNFHWD REAELHQREV GLRRTREELP RGSELHWERD
PGLRRGRELS LHWERDREAE LQWERDRQAE YWHRRATVAS YGPQGQDLLA FTFDPLPSGH
PAYPEASRSH AHSHLDMKYS SSSSGYQTPR QVCPCSPYQP SPSESRGYAS GYQSESTSPL
PPASAVMGHC GHSSGPAEHN HNHHHHHPDS QQSYSSDSHT DGLRSSGESV GWRDHITHGS
FKRVHRNGHA ACSTPSDMSG SPTPVHTSSP LRTQESPSPG RREYDIRTTD IISDYEAPQT
HEAHCHTNVI QESPDRQRSS TERLEPHTKE AQSHTASPKQ TESTNQCPAP TNLSPAAPQQ
QHCSSDMSSA RDSVTPTTTN QAHCQTPSSP VHTSPISDAH PHPTGPLQTF SPAGAGGPPS
EMSQPQSHTQ ATSSVGPSVA LVNGSSPTRE SHAEVPKHTS TTNPTSSPAP SSPQPGPSSM
DGSPVSDAPV PGFATLGRRL MLSGSDPHNH LNHTHGPPHH NYQASTEHSA AVDTNKRPCY
SPHTPQSYSS YTTISIPLPH PQPPLPEKRH LPGHSGSPSN GVKPAVGHVP ASTAPQHQHH
VTFSPTVGEI APPADQNDQV EAETANRVSV KFVQDSSKFW YKPSISREQA IAALKEREPG
TFLIRDSNSF QGAYGLALKV VTPPPNVSNH SNKVSDPLEQ LVRHFLIETS PRGVKIKGCQ
NEPYFGSLSA LVYQHSITPI SLPCALKILE KDLIGEVQEV QPVSNISTAA DLLKQGAACN
VLYLNSVETE SLTGPQAIAK ATDATLGRSP RPAATVVQFK VTSQGITLTD NQRRVFFRRH
YAVNSVTFSS IDPKDRRWTN SDNTTVKVFG FVAKKPGSTA ENVCHLFAEL DPDQPASAIV
NFINKVMLSQ RR
//
