ID A0A2K6QZT9_RHIRO Unreviewed; 1361 AA.
AC A0A2K6QZT9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tensin 2 {ECO:0000313|Ensembl:ENSRROP00000034317.1};
GN Name=TNS2 {ECO:0000313|Ensembl:ENSRROP00000034317.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000034317.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000034317.1}
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 STRING; 61622.ENSRROP00000034317; -.
DR Ensembl; ENSRROT00000058761.1; ENSRROP00000034317.1; ENSRROG00000040696.1.
DR GeneTree; ENSGT00940000161535; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:Ensembl.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0048871; P:multicellular organismal-level homeostasis; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
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); 2.
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 PRINTS; PR02045; F138DOMAIN.
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; 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:UP000233200};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..83
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 90..249
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 254..380
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1095..1202
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 146021 MW; DF28183F78AB1571 CRC64;
LDGGNQCSAK ARLLPSPRDE DGPTGNSHLC LKAEPHSFRE KVFRKKPPVC AVCKVTIDGT
GVSCRVCKVA THRKCEAKVA GDPPASVSQS AGVTGVSHCA RPALCFRGRF LLRIYLHLVP
HCWRSLLSKL FNLSEKRHDL TRLNPKVQDF GWPELHAPPL DKLCSICKAM ETWLSADPQH
VVVLYCKGSK GKLGVIVSAY MHYSKISAGA DQALATLTMR KFCEDKVATE LQPSQRRYIS
YFSGLLSGSI RMNSSPLFLH YVLVPTLPAF EPGTGFQPFL KIYQSMQLVY TSGVYHIAGP
GPQQLCISLE PALLLKGDVM VTCYHKVGRG TDRTLVFRVQ FHTCTIHGPQ LTFPKDQLDE
AWTDERFPFQ ASVEFVFSSS PEKIKGSTPR NDPSVSVDYN TTEPAVRWDS YENFNQHHED
SVDGSLTHTR GPLDGSPYAQ VQRPPRQTPP APSPEPPPPP MLSVSSDSGH SSTLTTEPAA
ESPGRPPPTA AERQELDRLL GGCGIASGGR GAGRETAILD DEEQPTVGGG PHLGVYPGHR
PGLSRHCSCR QGYRESCGVP NGGYYRPEGT LERRRLAYGG YEGSPQGYAE ASMEKRRLCR
SLSEGPYPCP PEMGKPATGD FGYRAPAYRE VVILEDPGLP ALYPCPACEE KLALPTAALY
GLRLEREAGE GWASEAGKPL LHPVRPGHPL PLLLPACGHH HAPMPDYSCL KSPKAGEEGH
EGCSYTMCPE GRYGHPGYPA LVTYSYGGAV PSYCPAYGRV PHSCGSPGEG RGYPSPGAHS
PRAGSISPGS PPYPQSRKLS YEIPTEEGGN RYPLPGHLAS AGPLASAESL EPVSWREGPS
GHSTLPRSPR DAPGSASSEL SGPSTPLHTS SPVQGKESTR RQDTRSPTSA PTQRLSSGEA
LPPVSQAGTG KAPELPSGSG PEPPAPSPVS PTFPPSSPSD WPQERSPGGL SDGTSPRSPV
PTTLPGLRHA PWQGPRGPPD SPDGSPLTPV PSQMPWLVAS PEPPQSSPTP AFPLAASYDT
NGLTQPPLPE KRHLPGPGQQ PGPWGPEQAS SPARGISHHV TFAPLLSDNV PQPPEPPTQD
SQSNVKFVQD TSKFWYKPHL SRDQAIALLK DKDPGAFLIR DSHSFQGAYG LALKVATPPP
SAQSWKGDPL EQLVRHFLIE TGPKGVKIKG CPSEPYFGSL SALVSQHSIS PISLPCCLHI
PSKDPLEETP EAPVPTNMST AADLLRQGAA CSVLYLTSVE TESLTGPQAV ARASSAALSC
SPRPTPAPRG PHFLAILSPP LSSEQHHLLQ PEVWKCASSH FFSFCRWTNP DGTTSKIFGF
VAKKPGSPWE NVCHLFAELD PDQPAGAIVT FITKVLLGQR K
//
