TENS1_BOVIN
ID TENS1_BOVIN Reviewed; 1715 AA.
AC Q9GLM4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tensin-1;
GN Name=TNS1; Synonyms=TNS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11023826; DOI=10.1042/bj3510403;
RA Chen H., Ishii A., Wong W.K., Chen L.B., Lo S.H.;
RT "Molecular characterization of human tensin.";
RL Biochem. J. 351:403-411(2000).
CC -!- FUNCTION: Involved in fibrillar adhesion formation. May be involved in
CC cell migration, cartilage development and in linking signal
CC transduction pathways to the cytoskeleton.
CC -!- SUBUNIT: Binds to actin filaments and interacts with phosphotyrosine-
CC containing proteins. Interacts with STARD8 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}. Cell junction, focal
CC adhesion. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localized at cell
CC periphery preferentially to fibrillar adhesions than focal adhesions.
CC Translocates from the cell edge to cell center in an ITGB1BP1-dependent
CC manner.
CC -!- PTM: Rapidly cleaved by calpain II. {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
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DR EMBL; AF225897; AAG33701.1; -; mRNA.
DR RefSeq; NP_777191.1; NM_174766.2.
DR AlphaFoldDB; Q9GLM4; -.
DR SMR; Q9GLM4; -.
DR STRING; 9913.ENSBTAP00000003229; -.
DR iPTMnet; Q9GLM4; -.
DR PaxDb; Q9GLM4; -.
DR PeptideAtlas; Q9GLM4; -.
DR PRIDE; Q9GLM4; -.
DR GeneID; 286798; -.
DR KEGG; bta:286798; -.
DR CTD; 7145; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR InParanoid; Q9GLM4; -.
DR OrthoDB; 172407at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0010761; P:fibroblast migration; IBA:GO_Central.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
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 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; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell junction; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..1715
FT /note="Tensin-1"
FT /id="PRO_0000215899"
FT DOMAIN 4..176
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 181..307
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1443..1552
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 398..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 863
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 906
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL0"
SQ SEQUENCE 1715 AA; 183508 MW; D32F16D64CEAF610 CRC64;
MSTSRTTEDS CELDLVYVTE RIIAVSFPST ANEENFRSNL REVAQMLKSK HGGNYLLFNL
SERRPDITKL HAKVLEFGWP DLHTPALEKI CSVCKAMDTW LNADPHNVVV LHNKGNRGRI
GVVIAAYMHY SNISASADHA LDRFAMKRFY EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN
NKPLFLHHVI MHGIPNFESK GGCRPFLRIY QAMQPVYTSG IYNVQGDSQT SICITIEPGL
LLKGDILLKC YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWHSYD NFNGHRDDGM EEVVGHTPGT
LDGSLYAKVK KKDSLHGSNG AVNATRPVLS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE
PAPGPASAPA ALSPEEKREL DRLLSGFGLE REKQGAMYHP QHLRSRPVGG PAAPSSGRHI
VPAQVHVRGG VLSVERETDI LDDELPNQDG HSVGSMGTLS SLDGVTNTSE GGYPEALSPL
TNGLDKPYPM EPMVNGGGYP YESASRAVSA QAGHTAPMRP SYSTQEGLAG YQREGPHPAW
PQSATTSHYG HDPNGMFRSQ SFPETEPQLP PAPARGGSSR EAVQRGLNSW QQQQQQQQQQ
QQPRPPPRQQ ERVHLESLGL SRPSPQPLAE PPMSGLPEFP RAASQQEIEQ SIEALNMLML
DLEPATAGAP LHKSQSVPGA WPGASPLSSQ PFSGSSCQSH PLTQSRSGYI PSGHSLGTPE
PAPRAPLESV PTGRPYSPYD YQPCPTGPNQ SYHPKSPATS SSSSFLPTTQ SSVGPQQPPA
SLPGLTTQPQ LPPKEVTSDP SRTPEEEPLN LEGLVAHRVA GVQAREKQPA EPPAPLRKRA
ASDGQYENQS PEPTSPRSPG VRSPVQCVSP ELALTIALNP GGRPKEPHLH SYKEAFEEME
GTSPTSPPPS GVRSPPGLAK TPLSALGLKP HNPADILLHP TGEPRSYVES VVRTAVAGPR
TQEPEPKSFS APAAQAYGHE TPLRIGTLGG SFVSPSPLST SSPILSADST SVGSFPSGES
SDQGARTPTQ PLLDSGFRSG SLGQPSPLAQ RNYQSSSPLP TAGSSYSSPD YSLQQFSSPE
GQARSQFSVA GVHTVPGSPQ ARHRTVGTNT PPSPGFGRRA VNPSLAAPSS PSLSHRQVMG
PLGTGFHGNT GSSPQSSAAT TPGSPSLGRH PGAQVSNLHG NVVTRPGSPS LGRHPGAHQG
TLASNLHSNA VASPGSPSLG RHLGGSGSVV PGSPSLDRHV PYGGYSTPED RRPTLSRQSS
ASGYQAPSTP SFPVSPAYYP GLSSPATSPS PDSAAFRQGS PTPALPEKRR MSMGDRAGSL
PNYATVNGKV SSSPVASGMS SPSGGSTVSF SHTLPDFSKY SMPDNSPETR AKVKFVQDTS
KYWYKPEISR EQAIALLKDQ EPGAFIIRDS HSFRGAYGLA MKVSSPPPTI MQQNKKGDMT
HELVRHFLIE TGPRGVKLKG CPNEPNFGSL SALVYQHSII PLALPCKLVI PNRDPTDESK
DSSGPANSTS DLLKQGAACN VLFVNSVDME SLTGPQAISK AISETLAADP TPAATIVHFK
VSAQGITLTD NQRKLFFRRH YPLNTVTFCD LDPQERKWTK TEGGAPAKLF GFVARKQGSA
TDNACHLFAE LDPNQPASAI VSFVSKVMLS AGQKR
