ID A0A286X845_CAVPO Unreviewed; 1347 AA.
AC A0A286X845;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Tensin 2 {ECO:0000313|Ensembl:ENSCPOP00000021588.1};
GN Name=TNS2 {ECO:0000313|Ensembl:ENSCPOP00000021588.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000021588.1, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000021588.1}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000021588.1};
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 EMBL; AAKN02014983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCPOT00000046026.1; ENSCPOP00000021588.1; ENSCPOG00000024457.2.
DR VEuPathDB; HostDB:ENSCPOG00000024457; -.
DR GeneTree; ENSGT00940000161535; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000024457; Expressed in hypothalamus and 13 other cell types or tissues.
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; 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:UP000005447};
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 116..274
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 279..405
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1093..1200
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 146276 MW; 4E44B68F4DAA50BA CRC64;
MKSSSPVERL LRALGRRDSS RATSRPKKAE PHSFREKVFR KKAPVCAVCK VTIDGTGVSC
RVCKVATHRK CEAKVTSSCQ ALPPAELSHS LAHQGSTKSL NHSKQRSTLP RSFSLDPLME
RRWDLDLTYV TERILAAAFP AQPEEQRHRG HLRELAHVLQ SKHRDKYLLF NLSEKRHDLT
RLNPKVQDFG WPELHAPPLD KLCSICKAME TWLSADAQHV VVLYCLGEAK ASSGADQALA
TLTMRKFCED KVATELHPSQ RRYISYFSGL LSGSIRMNSS PLFLHYVLVP MLPAFEPSTG
FQPFLKIYQS MQLVYTSGVY HISGPGPQQI CISLEPALLL KGDVMVTCYH KGSRGTDRTL
VFRVQFHTCT IHGPRLTFPK DQLDEAWADE RFPFQASVEF VFSSSPEKIK GNTPRNDPSI
SVDYNTAEPA VRWDSYENFN QHHEDSVDSS LTHTRGPLDG SPYAQVQRAP RQTPPAPSPE
PPPPPMLSVS SDSGHSSTLT TEPAAESPGR PPPTAAERLE LDRLLGGCGL ASGSRGAGRE
TAILDDEEQP SVSGGPHVGM YSTHREPCGV SNGGYYRPEG TLERRRLPYV SYEGPPQGYS
EAPVEKRRLC RSLSEGPYPY PPELAKPANG DFSYRGPGYR EVVILEDPGV SALCSCPTCE
EKLAVPTAAL YGLRLERETG EGWSSEAGKP LLHPVRPGHT LPLLVPAYGH HHAPMPDYSC
LKPPKAAEEA HEGCSYALCP ESRYGHPGFP ALVTYGYGGA VPSYCPAYGR VPHRCGSPGE
GRGHPSPGAH SPRAGSISPG SPPYPQPRKL SYEIPVEERG DKYPQASAGP SASTESPEPL
SWREGPSGHS TLPRSPRDAQ CSTSSELSGP STPLHTSSPV QGKESTRQQD TRSPISAPTH
RLSPSEALLP VSQGGPEKSP EQPARSGPEP QDSSPFSLTS SPSSPNNWPQ ERSPGGQSDS
ASPRGPVPTT LPGLRHAPWQ GPRGTPDSPD GSPLTPVPTQ MPWLVASPEP PQSSPIPAFP
LATSYETSGP TQPPLPEKRH LPGPGQQPGS WARGTSHHVT FAPLLLDATQ LPEPPTQESQ
SNVKFVQDTS KFWYKPHLSR DQAIALLKDK DPGAFLIRDS HSFQGAYGLA LKVATPPPSA
QPWKGDPLEQ LVRHFLIETG PKGVKIKGCP SEPYFGSLSA LVSQHSISPI SLPCCLCIPS
KGGQAPNSLD RGTCSVLYLT SVETESLTGP QAVAKASSAA LSCSPRPTPA VVHFKVSAQG
ITLTDNQRKL FFRRHYPVSS ITFSSIDPQD HRWTNPDGTT SKIFGFVAKK PGSPWENVCH
LFAELDPDQP AGAIVTFITK VLLGQRK
//
