ID A0A3Q2HAT7_HORSE Unreviewed; 1920 AA.
AC A0A3Q2HAT7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSECAP00000031185.2};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSECAP00000031185.2,
GN ECO:0000313|VGNC:VGNC:56615};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000031185.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000031185.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000031185.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000031185.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000031185.2};
RG Ensembl;
RL Submitted (JUL-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}.
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DR Ensembl; ENSECAT00000040932.3; ENSECAP00000031185.2; ENSECAG00000014711.4.
DR VGNC; VGNC:56615; TNS1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000002281; Chromosome 6.
DR Bgee; ENSECAG00000014711; Expressed in synovial membrane of synovial joint and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2HAT7; baseline.
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 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; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 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; 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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q2HAT7};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1920
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023927444"
FT DOMAIN 40..96
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 181..353
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 358..484
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1648..1757
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 154..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1920 AA; 204973 MW; F6E32D19F1C91714 CRC64;
MTRLSWCFSC VIRWGKYLFC LLPLRFCLRS QPEDLDAPKT HHFKVKTFKK VKPCGICRQA
ITREGCTCKV CSFSCHRKCQ AKLLASHRRG PVTAHCPCPG AQTPSPPSSS SARKVAAPCV
PPSSHELVPV NAESAPKNVV DTGEGVFRGG NTRKSLEEDG SARVPLSVQP HPQPIRNMSV
SRTPEDSCEL DLVYVTERII AVSFPSTANE ENFRSNLREV AQMLKSKHGG NYLLFNLSER
RPDIAKLHAK VLDFGWPDLH TPALEKICSV CKAMDTWLNA DPHNVVVLHN KGNRGRIGVV
IAAYMHYSNI SASANQALDR FAMKRFYEDK IVPIGQPSQR RYVHYFSGLL SGSIKMNNKP
LFLHHVIMHG IPNFESKGGC RPFLRIYQAM QPVYTSGIYN VQGDSQTSIC ITIEPGLLLK
GDILLKCYHK KFRSPARDVI FRVQFHTCAI HDLGVVFGKE DLDDAFKDDR FPEYGKVEFV
FSYGPEKIQG MEHLENGPSV SVDYNTSDPL IRWDSYDNFN GPRDDGMEEV VGHTQGPLDG
SLYAKVKKKD SLHGSTGAVN ATRPALSATP NHVEHTLSVS SDSGNSTAST KTDKTDEPGP
GPSGAPAALS PEEKRELDRL LSGFGLEREK QGAMYHAQHL RSRPAGRPAA PSSGRHVVPA
QVHVNGGALA SERETDILDD ELPNQDGHSV GSMGTLSSLD GVTNTSEGGY PEAMSSLTNG
LDKPYPVEPM VNGGGYPYES ASRAVPAHAG HTAPMRPSYS TQEGLAGYQR EGPHPAWSQP
MTTSPYGHDP SGMFRSQSFP EAEPQLPPAP ARGGSSREAV QRGLSSWQQQ QQQQQPPLQQ
PRPPPRQQER AHLESLGLSR PSPQPLAETP TPGLPEFPRA ASQQEIEQSI ETLDMLMLDL
EPAAAAAPLH KSQSVPGAWP GASPLSSQPF SGSSCQSHPL TQSRSGYIPS GHSLGTPEPA
PRASLESIPP GRPYSPYDYQ PCPAGPNQSF RPKSPASSSS SSAFLPTAQG PPGPQQPPAS
LPGLTAQPQL PPKEAASDPS RTPEEEPLNL EGLVAHRVAG VQAREKQPAE PPAPLRRRAA
SDGQYENQSP EPPSPRSPGV RSPVQCVSPE LALTIALNPG GRPKEPHLHS YKEAFEEMEG
TSPSSPPPSG VRSPPGLAKT PLSALGLKPH NPADILLHPT GEPRSYVESV VRTAVAGPRV
QDPEPKSFSA PAAQAYGHET PLRNGTLGGS FVSPSPLSTS SPILSADSTS VGSFPSGESS
DQGRRTPTQP LLDSGFRSGS LGQPSPSAQR SFQSPSPLAT VGSSYSSPDY SLQQFSSPES
QAPSQFSVAS VHTVPGSPQA RHRTVGTNTP PSPGFGRRAV NSGMAAPGSP SLSHRQVMGP
PGTGFHGNTI SSPQGSAATT PGSPSLGRHP GAHQVSGLHG NVATTPGSPS LSRHPGAHQA
SGLHGNVVTT PGSPSLGRHP GAHQGNLASG LHGNAIASPG SPSLGRHLGG SGSVVPGSPS
LDRHVAYGGY STPEDRRPTL SRQSSASGYQ APSTPSFPVS PAFYPGLSSP ATSPSPDSAA
FRQGSPTPAL PEKRRMSVGD RAGSLPNYAT VNGKVSSSPV ASGMSSPSGG STVSFSHTLP
DFSKYSMPDN SPETRAKVKF VQDTSKYWYK PEISREQAIA LLKDQEPGAF IIRDSHSFRG
AYGLAMKVSS PPPTIMQQNK KGDMTHELVR HFLIETGPRG VKLKGCPNEP NFGSLSALVY
QHSIIPLALP CRLVIPNRDP TDESKDSSGP ANSTTDLLKQ GAACNVLFIN SVDMESLTGP
QAISKATSET LAADPTPTAT IVHFKVSAQG ITLTDNQRKL FFRRHYPLNT VTFCDLDPQE
RKWMKTEGGA PAKLFGFVAR KQGSTTDNAC HLFAELDPNQ PASAIVNFVS KVMLSAGQKR
//