ID A0A3Q2HCA7_HORSE Unreviewed; 1582 AA.
AC A0A3Q2HCA7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSECAP00000030955.2};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSECAP00000030955.2,
GN ECO:0000313|VGNC:VGNC:24402};
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:ENSECAP00000030955.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000030955.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030955.2,
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:ENSECAP00000030955.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030955.2};
RG Ensembl;
RL Submitted (NOV-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; ENSECAT00000049319.3; ENSECAP00000030955.2; ENSECAG00000020052.4.
DR VGNC; VGNC:24402; TNS3.
DR GeneTree; ENSGT00940000156328; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000002281; Chromosome 4.
DR Bgee; ENSECAG00000020052; Expressed in articular cartilage of joint and 23 other cell types or tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14561; PTP_tensin-3; 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 InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF5; TENSIN-3; 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; PS50056; TYR_PHOSPHATASE_2; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1582
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040424833"
FT DOMAIN 52..100
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 130..302
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 235..291
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 307..433
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1309..1419
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 111..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 169645 MW; 772924B6090DCE97 CRC64;
MKLFFWMGGT ELLILPVLQV DLQEPAVRPP GFHQWGNGGR EAACPEELAS SLHSFKNKAF
KKAKVCGVCK QIIDGQGSSC RACKYSCHKK CEAKVVIPRC VQVPPEQAPV GSSPPASLCG
DKPSRPAALN PTMEDGRELD LTYITERIIA VSFPAGCSEE SYLHNLQEVT RMLRSKHGDN
YLVLNLSEKR YDLTKLNPKI LDVGWPELHA PPLDKVCTIC KAQESWLNSD PQHVVVIHCR
GGKGRIGVVI SSYMHFTNVS ASADQALDRF AMKKFYDDKV STLMQPSQKR YVQFLSGLLS
GTVKMNASPL FLHFVILHGI PNFDTGGVCR PFLKLYQAMQ PVYTSGIYNI GPENQSRIYI
AIEPAQLLKG DIMVKCYHKK YRSATRDVIF RLQFHTGAVQ GYGLVFGKED LDNASQDDRF
PDDGKIELVF SATPERIQGC EHLRNDHGVI VDFNTADPLI RWDSYENLSA DGEVLHTQGP
VDGSLYAKVR KKSASDPSVP GGAPAIPASS PDHGDHTLSV SSDSGHSTAS VRTDRTEEHL
APGPKRGLSP QEKAELDQLL SGFGLEDSGS PLKDMTDAHS KYSGTRHVVP AQVHVNGDAT
PKDRETDILD DEMPSHDLHS VDSIGTLSSS EGHQSAHLGP FTCHQSSQNS LLSDGFGSGT
GEDQHSTLAP DLGLGVDTLY ERERAFGSRE PKQPQPVLRK PSVSPQMPAY GQGSYSTQTW
VRQQQMVAAH HYSFAPDGDA RLSSRGPADS SILAQAQPRV PVTPTRGASS KVAVQRGIGP
GPHAPDTQRP PPGKVFKPRF PDVKVMNGTG LEQSADPSPG SPTLDIDQSI EQLNRLILEL
DPTFEPIPTH INTLGGQTNG PVPPDSMGGG LRASGRLQDT GEGPSRAPAR QATSGDEPLG
VRFRKLSIGQ YDNSAEGQPA FSKCGWGKAT SADQAPSLAP FLSPTDTKEM VVTAYPPDLD
GIDGRIFSPT KSGSESISST PAFPVSPETP YVTASPHHPP FSPPRPQMGS AGSLYKGAHE
PRGCPELLSH PVGMSESPAG PNPAMLRADM PPAPSFQRAF PSSCTTASSS PGQRRESPSS
AEHQWVETSP KSTLTLLGSG RPAGGLLSAS EFPGPGKDSP ARPHFPPVEL QASFHSHELS
LAEPPEALGP PSGQAFLSFG AAPMGSGLPP GEDPGAVLAN SHSASQAPGT PRTAAAAADN
GFLSHNFLTV APGHSGHHSP VLQGQGLTLP GQPPLPEKKR ASEGDRSFGS VSPSSSGFSS
PHSGSTMSIP FPNVLPDFSK ASEAAAPSPD NPGDKHVSVN FVQDTSKFWY KADISREQAI
AMLKDKEPGS FIVRDSHSFR GAYGLAMKVA TPPPSVLQMN KKAGDLANEL VRHFLIECTP
KGVRLKGCSN EPYFGSLTAL VCQHSITPLA LPCKLLIPDR DPLEEIAESS PQTAANSAAE
LLKQGAACNV WYLNSVEMES LTGHQAVQKA LSITLVQEPP PLSTVVHFKV SAQGITLTDN
QRKLFFRRHY PVSSVIFCAL DPQDRKWIAD GPSSRVFGFV ARKQGSATDN VCHLFAEHDP
EQPASAIVNF VSKVMIGSPK KI
//
