ID D2HLP0_AILME Unreviewed; 1382 AA.
AC D2HLP0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Tensin 2 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=PANDA_012429 {ECO:0000313|EMBL:EFB17402.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB17402.1};
RN [1] {ECO:0000313|EMBL:EFB17402.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL193014; EFB17402.1; -; Genomic_DNA.
DR InParanoid; D2HLP0; -.
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 SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..55
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 98..270
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 275..401
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1113..1220
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 437..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFB17402.1"
FT NON_TER 1382
FT /evidence="ECO:0000313|EMBL:EFB17402.1"
SQ SEQUENCE 1382 AA; 149212 MW; 395BD793C13D85EF CRC64;
QPRKAEPHSF REKVFRKKPP VCAVCKVTID GTGVSCRVCK VATHRKCEAK VTSSCQALPP
AELRRNTAPV RRIEHLGSTK SLNHSKQRST LPRSFSLDPL MERRWDLDLT YVTERILAAA
FPARPDEQRH RGHLRELAHV LQSKHRDKYL LFNLSEKRHD LSRLNPKVQD FGWPELHAPP
LDKLCSICKA METWLSADPQ HVVVLYCKGS KGKLGVIVSA YMHYSKISAG ADQALATLTM
RKFCEDKVAA ELQPSQRRYI SYFSGLLAGS IRMNSSPLFL HYVLVPVLPA FEPGTGFQPF
LKIYQSMQLV YTSGIYHIAG PGPQQLCISL EPALLLKGDV MVTCYHKGGR GTDRTLVFRV
QFHTCTIHGP RLTFPKDQLD EAWADERFPF QASVEFVFSS SPEKIKGNTP RNEPSVSVDY
NTAEPAVRWD SYENFNQHHE DSVDGSPTHT RGPLDGSPYA QVQRAPRQTP PAPSPEPPPP
PMLSVSSDSG HSSTLTTEPA AESPGRPPPT AAERQGGLGG CGVAGGGRGA GRETAILDDE
EQPPAGGGPH LGMYSGHRPG LSRHCSCRQG YREPCGVPNG GYYRPEGTLE RRRLAYGGYE
GHPQGYAEAS VEKRRLCRSL SEGPYPYPPE LGKPANGDFG YRAPGYREVV ILEDAGLPAL
CSCPACDEKL ALPTAALYGL RLEREAGEGW AGEAGKPLLH PVRPGHPLPL LVPACGHHHA
PMPDYSCLKP PKVGDDGHEG CPYAVCPEGR YGHPGYPALV TYGYGGAVPS YCPAYGRVPH
SCGSPAEARA YSSSGAHSPR AGSVSPGSPP YPQSRKLSYE IPAEEGGDRY PMPGHLAPAG
PLASAESPEP ASWREGPSGH STLPRSPRDA PCSASSELSG PSTPLHTSSP VQGKESTRRQ
DSTSPTLVPT QRLSPGEALP SIPQGGAEKA SELPARSGLE LPAASPFSPT SPPSSPNDWP
QEKSPGSRSD SASPRGPVPT TLPGLRHAPW QGLRDPPDSP DGSPLTPVPT QMPWLVASSE
PPQSSPTPAF PLAASYDING PTQPPLPEKR HLLGPGQQPG PWGSEQASPP ARGTSHHVTF
APLLPDNVPQ PPEPPMQESQ SNVKFVQDTS KFWYKPHLSR DQAIALLKDK DPGAFLIRDS
HSFQGAYGLA LKVATPPPSA QPWKGDPLEQ LVRHFLIETG PKGVKIKGCP SEPYFGSLSA
LVSQHSISPL SLPCCLRIPS KEPLEETPEA PVPANMSTAA DLLRQGAACS VLYLTSVETE
SLTGPQAVAR ASSAALSCSP RPTPAIVHFK VSAQGITLTD NQRKLFFRRH YPVNSITFSS
TDPQDRRWAN PDGTTSKIFG FVAKKPGSPW ENVCHLFAEL DPDQPAGAIV TFITKVLLGQ
RK
//
