ID A0A498MRY7_LABRO Unreviewed; 1812 AA.
AC A0A498MRY7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Tensin-1 isoform X3 {ECO:0000313|EMBL:RXN23220.1};
GN ORFNames=ROHU_023035 {ECO:0000313|EMBL:RXN23220.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN23220.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN23220.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN23220.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN23220.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN23220.1}.
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DR EMBL; QBIY01012564; RXN23220.1; -; Genomic_DNA.
DR STRING; 84645.A0A498MRY7; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
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:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20888; C1_TNS1_v; 1.
DR CDD; cd01213; PTB_tensin; 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:SF3; TENSIN-1; 1.
DR Pfam; PF00130; C1_1; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MRY7};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 16..63
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 139..311
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 316..442
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1542..1651
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 106..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1812 AA; 196487 MW; F0BFBD1657C93C63 CRC64;
MSENTGKPEE FEAVHSHTFR LKTFKKGKHC GVCKQTVNNE GLICRVCRLA CHRKCEVKVS
SSCVPVANYE LAPSNDLPLK HIETTMFRPV YSCFGCYCSL LRHHGRRTPP SPQGSLTGST
KSSKSMESRR RPSRSLSLIQ AMEENYEVDL VYITERIISV TFPSNVEEPS YSANIKEVAT
MLRSKHGDNY LVFNLSEKRY DISKLNPKVL DFGWPDHHAP ALDKICSICK AMDTWMNADS
HNVVVLHNKG NRGRTGVVVA AYMHYSNISA SADQALDRFA MKRFYEDKVL PVGQPSQRRY
VQYFSGLLSG HIKINNKPLF LHHVIMHGIP NFESKGGCRP FLKIYQAMQP VYTSGIYNVQ
GDSQTSICIT IEPGLLLKGD ILLKCYHKRF RSPSRDVIFR VQFHTCAVHD LGIVFGKDEL
DETFKDDRFP EYGKVEFVFS FGPEKIQGMD HLENGPSVSV DYNTQDPLIR WDSYENFNQR
CEDSAEDVIH TQGPLDGSLY AKVRKKESLD GGVTTNGLPA TVDHTLPAVD HTLPPVDHAL
SVSSDSGNST ASIKTDRTDE VSHQPALVSQ PSSQPLSPEE KQELDQLLSG LEAPMHRAGY
QSSPGTGGGG VLHLVPAQVH VNGHTNIDRE TDILDDDLPN SQEGNSVDSL GTLSSFEGRA
TPADLYYQSE TVINGQDAPY SEKGVHEKIP EPKVHSSSSV QEHLGSASGY ANQNGNIYRS
QSLGATPTTE QKYMPKAPTR TTSSRDAVQR GLNVWQQYGV PEVPVTDGVT FNPVLQSHSL
PEFPHMASQQ EIEQSIEALN MLMLDLDPAL TQVPKSHSAP SGEGGVVTTQ PSFSQTQARP
SYQSDAAIHD RSGASPYPLS FQQVAAEQPT INQQRPTAMS QHAPFPSEAE GQAPMSRSTV
PSSTFGVLQL KPLNIYPSST TSQSPEPQES QHSYSASSSP LPKESEPEDA NYKLDGLVAH
RVAGKINFPL SLLSGVQSGE MSPDEVSVPG RCRTISEGLS QDDSSPTPGS SVRSPIRCIS
PELANTIALN PGGRPKERHM HSYREAFEEM DGGPVSPPPI VGGEALPQTP AFPVSPQTPY
FNLSRSPPGL AKTPLSFLGL KPHNPAEILL NQTGSEPRSY VESVAKAAAS GPPASPVSST
YDSDSLARPA GPSHAYNAPL SSSSPIQSPD AVESTLTDSG VGLNSLSQAA VDSVLHSQPS
ESTYQTPIPS YPTSSSMLGG YMTPDISPSL PEAIQNNATT IHPLAGSPGT RHQAVLPDMM
SAPGFQHRMP NQDGPVLGRQ PIPANGHLPG MAGSPVQGRH TMVSQGTQSS PILSRQYPVT
QGSQSSPILS RQPMGQAVHS SPVLNRQASL NQPIVLPNQS SPVLSRQPSV TQPNQGSPVL
SRQSSLTHPS QGSPILGHHP SLTQGSPSLD RHPMYSGYTT PEERHGALSR QSSSSGYQAP
STPSFPVSPA GYIDGVGFRQ GSPVPQPQLP EKRRMSSSDR SNGGLSYGTL NGKMSSPVSS
GGSTPSVHFF HTLPDFSKLN MCDGSPETRL NVKFVQDTSK FWYKPDISRD QAINMLKDQD
PGAFVIRDSH SFRGAYGLAM KVASPPPTAQ PTKKAGDVTN ELVRHFLIET SPKGVRLKGC
PNEPYFGCLS ALVYQHSITP LALPCKLVIP TRDPLEESPE IATPTNPAAE MLKQGAACNV
LYINSVDMES LTGPQAIAKA ISETMAAGPA PSATIVHFKV SAQGITLTDN QRKLFFRRHY
PISTVTFCDI DPQERKWSKP EGGNAKFFGF VARKQGSTTD NVSHLFAEMD PDQPATAIVN
FVSKVMLNSQ KR
//
