ID A0A3Q1MYX6_BOVIN Unreviewed; 1409 AA.
AC A0A3Q1MYX6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tensin 2 {ECO:0000313|Ensembl:ENSBTAP00000061338.1};
GN Name=TNS2 {ECO:0000313|Ensembl:ENSBTAP00000061338.1,
GN ECO:0000313|VGNC:VGNC:36208};
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 {ECO:0000313|Ensembl:ENSBTAP00000061338.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000061338.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000061338.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000061338.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000061338.1};
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 PaxDb; 9913-ENSBTAP00000009070; -.
DR Ensembl; ENSBTAT00000071970.1; ENSBTAP00000061338.1; ENSBTAG00000006904.6.
DR VEuPathDB; HostDB:ENSBTAG00000006904; -.
DR VGNC; VGNC:36208; TNS2.
DR GeneTree; ENSGT00940000161535; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000006904; Expressed in bone marrow and 104 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MYX6; baseline and differential.
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; cd20887; C1_TNS2; 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 PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF1; TENSIN-2; 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; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..79
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 122..294
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 299..425
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1140..1247
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 465..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 152406 MW; F1AB466E1054DCFE CRC64;
MGSPQTTEEG VQPSVPRWVA LCVVKPRKAE PHSFREKVFR KKPPVCAVCK AAIDGTGVSC
RVCKVATHRK CEAKVTSSCQ ALPPVELRRN TAPVRRIEHL GSTKSLNHSK QRSTLPRSFS
LDPLMERRWD LDLTYVTERI LAASFPARPD EQRHRGHLRE LAHVLQSKHR DKYLLFNLSE
KRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGSKGKLGV
IVSAYMHYSK ISAGADQALA TLTMRKFCED KVAAELQPSQ RRYITYFSGL LSGSIRMNSS
PLFLHHVLVP VLPAFEPGAG FQPFLKIYQS MQLVYTSGIY HIAGPGPQQL CISLEPALLL
KGDVMVTCYH KGSRGTDRTL VFRVQFHTCT IHGPRLTFSK DQLDEAWTDE RFPFQASVEF
VFSSSPEKIK GNTPQNEPSV SVDYNTAEPA VRWDSYENFN LHHEDSADDS VTHTRGPLDG
SPYAQVQRAP RQTPPAPSPE PPPPPLLSVS SDSGHSSTLT TEPAAESPGR PPPTAAERQE
LERLLGGCGV ASGGRGAGRE TAILDDEDQP AAGGGPHLGI YSGHRPGLSR HCSCRQGYRE
PCGVPNGGYY RPEGTLERRR LAFGAYEGPP QGYAEPSVEK RRLCRSLSEG PYPYPSELGK
PANGDFGYRP PGYREVVILE DPGLPPLCSC PACEEKLALP TAALYGLRLE REAGEGWASE
AGKPLLHPVR PGHPLPLLVP ACGHHHTPLP DYSCLKPPKA GEEGHEGCSY ALCPEGRYGH
PGYPALVTYG YGGAVPSYCP AYGRVPHSCG SPGEGRGYPS PRAHSPRAGS ISPGSPPYPQ
SRKLSYEIPA EEGGDRYLLP GHLAPAGPLA SAESPEPVSW REGPSGHSTL PRSPRDAQCS
AASELSGPST PLHTSSPVQG KESARRQDTR SPTLAPTQRL SPAEALPPVS QGGADKAPEL
PARSGPEPPA PGAFSLASPP SSPNDWPQER SPGGRSDSAS PRGPVPNTLP GLRHAPWQGL
RDPPDSPDGS PLTPVPTQMP WLVASPEPPQ SSPTPAFPLA ASYDINGAPQ PPLPEKRHLL
GPGQQPGPWG PEQASPPARG ASHHVTFAPL LPDNTPQPPE PPMQESQSNV KFVQDTSKFW
YKPHLSRDQA ITLLKDKDPG AFLIRDSHSF QGAYGLALKV ATPPPSAQSW KGDPSEQLVR
HFLIETGPKG VKIKGCPSEP YFGSLSALVS QHSISPLSLP CCLRIPSKDP LEEVPEAPVP
SNMSTAADLL RQGAACSVLY LTSVETESLT GPQAVARASS AALSCSPRPT PAVVHFKVSA
QGITLTDNQR KLFFRRHYPV NSITFSSTDP QDRRWTNSDG TTSKIFGFVA KKPGSPWENV
CHLFAELDPD QPAGAIVTFI TKVLLGQRK
//
