ID A0A2K6GR55_PROCO Unreviewed; 1345 AA.
AC A0A2K6GR55;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tensin 2 {ECO:0000313|Ensembl:ENSPCOP00000028707.1};
GN Name=TNS2 {ECO:0000313|Ensembl:ENSPCOP00000028707.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000028707.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000028707.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSPCOT00000039640.1; ENSPCOP00000028707.1; ENSPCOG00000027013.1.
DR GeneTree; ENSGT00940000161535; -.
DR Proteomes; UP000233160; Unplaced.
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:UP000233160};
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 1076..1183
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Basic and acidic residues"
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 827..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..970
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 146159 MW; CEF43662E0F31280 CRC64;
MKSSGPVERL LRALGRRDSS RATSRPRKAE PHSFREKAFR KKPPVCAVCK VTIDGTGVSC
RVCKMATHRK CEAKVTSSCQ ALPPAELRRN TAPVRRIEHL GSTKSLNHSK QRSSLPRSFS
LDPLMERRWD LDLTYVTERI LAAAFPARPD EQRHRGHLRE LAHVLQSKHR DKYLLFNLSE
RRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGSKGKLGV
IVSAYMHYSK ISAGADQALA TLTMRKFCED KVATELQPSQ RRYISYFSGL LSGSIRMNSS
PLFLHYVLVP MLPAFEPGTG FQPFLKIYQS MQLVYTSGVY HIAGPGPPQL CISLEPALLL
KGDVMVTCYH KGGRGTDRTL VFRVQFHTCT IHGPRLAFPK DQLDEAWTDE RFPFQASVEF
VFSSSPEKVK GSTPRNDPSV SVDYNTTEPA VRWDSYENFN QYHEDSVDGS LTHTRGPLDG
SPYAQVQRAP RQTPPAPSPE PPPPPMLSVS SDSGHSSTLT TEPAAESPGR PPPTAAERQE
LDRLLGGCGV ASGGRGAGRE TAILDDEEQP PMGGGPHLGV YSGHRPGLSR HCSCRQGYRE
PCGVPNGGYY RPEGTLERRR LAYGGYEGPP QGYAEASMEK RRLCRSLSEG PYPYAPEPMG
KQANGDFSYR SPGYREVVIL EDPVLPALCS CPACEEKLAL PTAALYGLRL EREAGEGWAS
EAGKPLLHPV RPGHPLPLLV PAYGHHHAPM PEYNCLKPPK AGEEGHEGCS YTMCPEGRKL
SYEIPAEEGG SRYPLPGHLA SAGPLASAES PEPVSWREGP SGHSTLPRSP REAQCGASSE
LSGPSTPLHT SSPVQGKEST RRQDTRSPTL APTQRLGPGE ALPPVSQGSP GKAPELPARS
GPEPPASSLC SPTSPPSSPN DWPQERSPGG RSDSASPQGP VPTTLPGLRH TPWQGPQGPP
DSPDGSPLTP VPTQVPWLVA SPEPPQSSPT PAFPLAAAYD TNGPTQPPLP EKRHLPGPGQ
QPGPWGPEQA SPPARGTSHH VTFAPLLPDN APQLPEPPMQ ESQSNVKFVQ DTSKFWYKPH
LSRDQAIALL KDKDPGAFLI RDSHSFQGAY GLALKVATPP PSAQPWKGDP LEQLVRHFLI
ETGPKGVKIK GCPSEPYFGS LSALVSQHSI SPISLPCCLR IPSKDPLEET PEAPVPSNMS
TAADLLRQGA ACSVLYLTSV EMESLTGPQA VARASSAALS CSPRPTPAVV HFKVSTQGIT
LTDNQRKLFF RRHYPVNSIT FSSTDPQDRR WTNPDGTASK IFGFVAKKPG SPWENVCHLF
AELDPDQPAG AIVTFITKVL LGQRK
//
