ID A7E2A6_HUMAN Unreviewed; 1409 AA.
AC A7E2A6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Tensin like C1 domain containing phosphatase (Tensin 2) {ECO:0000313|EMBL:AAI50260.1};
GN Name=TENC1 {ECO:0000313|EMBL:AAI50260.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI50260.1};
RN [1] {ECO:0000313|EMBL:AAI50260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC150259; AAI50260.1; -; mRNA.
DR PeptideAtlas; A7E2A6; -.
DR ChiTaRS; TNS2; human.
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; cd14562; PTP_tensin-2; 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 2: Evidence at transcript level;
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 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..1251
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..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 895..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1034
FT /note="Pro 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; 152596 MW; 0B9899FF93508854 CRC64;
MKSSGPVERL LRALGRRDSS RAASRPRKAE PHSFREKVFR KKPPVCAVCK VTIDGTGVSC
RVCKVATHRK CEAKVTSACQ ALPPVELRRN TAPVRRIEHL GSTKSLNHSK QRSTLPRSFS
LDPLMERRWD LDLTYVTERI LAAAFPARPD EQRHRGHLRE LAHVLQSKHR DKYLLFNLSE
KRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGNKGKLGV
IVSAYMHYSK ISAGADQALA TLTMRKFCED KVATELQPSQ RRYISYFSGL LSGSIRMNSS
PLFLHYVLIP MLPAFEPGTG FQPFLKIYQS MQLVYTSGVY HIAGPGPQQL CISLEPALLL
KGDVMVTCYH KGGRGTDRTL VFRVQFHTCT IHGPQLTFPK DQLDEAWTDE RFPFQASVEF
VFSSSPEKIK GSTPRNDPSV SVDYNTTEPA VRWDSYENFN QHHEDSVDGS LTHTRGPLDG
SPYAQVQRPP RQTPPAPSPE PPPPPMLSVS SDSGHSSTLT TEPAAESPGR PPPTAAERQE
LDRLLGGCGV ASGGRGAGRE TAILDDEEQP TVGGGPHLGV YPGHRPGLSR HCSCRQGYRE
PCGVPNGGYY RPEGTLERRR LAYGGYEGSP QGYAEASMEK RRLCRSLSEG LYPYPPEMGK
PATGDFGYRA PGYREVVILE DPGLPALYPC PACEEKLALP TAALYGLRLE REAGEGWASE
AGKPLLHPVR PGHPLPLLLP ACGHHHAPMP DYSCLKPPKA GEEGHEGCSY TMCPEGRYGH
PGYPALVTYS YGGAVPSYCP AYGRVPHSCG SPGEGRGYPS PGAHSPRAGS ISPGSPPYPQ
SRKLSYEIPT EEGGDRYPLP GHLASAGPLA SAESLEPVSW REGPSGHSTL PRSPRDAPCS
ASSELSGPST PLHTSSPVQG KESTRRQDTR SPTSAPTQRL SPGEALPPVS QAGTGKAPEL
PSGSGPEPLA PSPVSPTFPP SSPSDWPQER SPGGHSDGAS PRSPVPTTLP GLRHAPWQGP
RGPPDSPDGS PLTPVPSQMP WLVASPEPPQ SSPTPAFPLA ASYDTNGLSQ PPLPEKRHLP
GPGQQPGPWG PEQASSPARG ISHHVTFAPL LSDNVPQTPE PPTQESQSNV KFVQDTSKFW
YKPHLSRDQA IALLKDKDPG AFLIRDSHSF QGAYGLALKV ATPPPSAQPW KGDPVEQLVR
HFLIETGPKG VKIKGCPSEP YFGSLSALVS QHSISPISLP CCLRILSKDP LEETPEAPVP
TNMSTAADLL RQGAACSVLY LTSVETESLT GPQAVARASS AALSCSPRPT PAVVHFKVSA
QGITLTDNQR KLFFRRHYPV NSITFSSTDP QDRRWTNPDG TTSKIFGFVA KKPGSPWENV
CHLFAELDPD QPAGAIVTFI TKVLLGQRK
//
