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Database: UniProt
Entry: A0A3Q2HAT7_HORSE
LinkDB: A0A3Q2HAT7_HORSE
Original site: A0A3Q2HAT7_HORSE 
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
//
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