ID A0A2R9B4X9_PANPA Unreviewed; 1419 AA.
AC A0A2R9B4X9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Tensin 2 {ECO:0000313|Ensembl:ENSPPAP00000024637.1};
GN Name=TNS2 {ECO:0000313|Ensembl:ENSPPAP00000024637.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000024637.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000024637.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000024637.1}
RP IDENTIFICATION.
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; AJFE02109855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003831089.1; XM_003831041.2.
DR STRING; 9597.ENSPPAP00000024637; -.
DR Ensembl; ENSPPAT00000047462.1; ENSPPAP00000024637.1; ENSPPAG00000035457.1.
DR GeneID; 100992860; -.
DR CTD; 23371; -.
DR GeneTree; ENSGT00940000161535; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000240080; Chromosome 12.
DR Bgee; ENSPPAG00000035457; Expressed in heart and 6 other cell types or tissues.
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; 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 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:UP000240080};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 41..89
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 132..304
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 309..435
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1150..1257
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 472..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..996
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 153592 MW; 9060CF5D1C892C19 CRC64;
MDGGGVCVGR GDLLSSPQAL GQLLRKESRP RRAMKPRKAE 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 PAHPLPLLLP ACGHHHAPMP DYSCLKPPKA GEEGHEGCSY
TMCPEGRYGH PGYPALVTYS YGGAVPSYCP AYGRVPHSCG SPGEGRGYPS PGAHSPRAGS
ISPGSPPYPQ SRKLSYEIPT EEGGDRYPLP GHLASAGPLA SAESLEPVSW REGPSGHSTL
PRSPRDAPCS ASSELSGPST PLHTSSPVQG KESTRRQDTR SPTSAPTQRL SPGEALPPVS
QAGTGKAPEL PSGSGPEPPA PSPVSPTFPP SSPSDWPQER SPGGHSDGAS PRSPVPTTLP
GLRHAPWQGP RGPPDSPDGS PLTPVPSQMP WLVASPEPPQ SSPTPAFPLA ASYDTNGLSQ
PPLPEKRHLP GPGQQPGPWG PEQASSPTRG ISHHVTFAPL LSDNVPQTPE PPTQESQSNV
KFVQDTSKFW YKPHLSRDQA IALLKDKDPG AFLIRDSHSF QGAYGLALKV ATPPPSAQPW
KGDPVEQLVR HFLIETGPKG VKIKGCPSEP YFGSLSALVS QHSISPISLP CCLRIPSKDP
LEETPEAPVP TNMSTAADLL RQGAACSVLY LTSVETESLT GPQAVARASS AALSCSPRPT
PAVVHFKVSA QGITLTDNQR KLFFRRHYPV NSITFSSTDP QDRRWTNPDG TTSKIFGFVA
KKPGSPWENV CHLFAELDPD QPAGAIVTFI TKVLLGQRK
//
