ID A0A455B5I5_PHYMC Unreviewed; 1889 AA.
AC A0A455B5I5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Tensin-1 isoform X1 {ECO:0000313|RefSeq:XP_028339276.1};
GN Name=TNS1 {ECO:0000313|RefSeq:XP_028339276.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028339276.1};
RN [1] {ECO:0000313|RefSeq:XP_028339276.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028339276.1};
RG RefSeq;
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 RefSeq; XP_028339276.1; XM_028483475.2.
DR KEGG; pcad:102996323; -.
DR InParanoid; A0A455B5I5; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000248484; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14560; PTP_tensin-1; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 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; IPR035892; C2_domain_sf.
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 InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 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; 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.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 68..240
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 245..371
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1617..1726
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 18..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1889 AA; 201748 MW; 60E71C578673BA08 CRC64;
MFALRPHAVF SLYPQPVNTE TAPKNVVDTG EGASRGGNTR KSLEEDSSTR VTPSVQPHPQ
PIRNMSVSRA ADDSCELDLV YVTERIIAVS FPSTANEENF RSNLREVAQM LKSKHGGNYL
LFNLSERRPD ITKLHAKVLE FGWPDLHTPA LEKICSVCKA MDTWLNADPH NVVVLHNKGN
RGRIGVVIAA YMHYSNISAS ADQALDRFAM KRFYEDKIVP IGQPSQRRYV HYFSGLLSGS
IKMNNKPLFL HHVIMHGIPN FESKGGCRPF LRIYQAMQPV YTSGIYNVQG DSQTSICITI
EPGLLLKGDI LLKCYHKKFR SPARDVIFRV QFHTCAIHDL GVVFGKEDLD DAFKDDRFPE
YGKVEFVFSY GPEKIQGMEH LENGPSVSVD YNTSDPLIRW DSYDNFNGHQ DDGMEEVVGH
TQGPLDGSLY AKVKKKDSLH GSTGAVNATR PALSATPNHV EHTLSVSSDS GNSTASTKTD
KTDEPAPGPS SAPAALSPEE KRELDRLLSG FGLEREKQGT MYHTQHLRSR LAGGPAAPSS
GRHVVPAQVH VNGRALASER ETDILDDELP NQDGHSVGSM GTLSSLDGVT NTSEGGYPEA
LSPLTNGLDK PYPVEPMVNG GGYPYESASR AVPAQAGHPA PMRPSYSAQE SLAGYQQEGP
HPAWPQSMTT SHYGHDPSGM FRSQSFPETK PQLPPAPARG GSSREAVQRG LNSWQPHPPP
RQQERAHLES LGLSRPSPQP LAEPPMPGLP EFPRAASQQE IEQSIEALNM LMLDLEPATA
AAPLHKSQSV PGAWPGASPL SSQPLSGSSS QSHPLTQSRS GYIPSGHSLG TPEPAPRASL
ESVPPGRPYS PYDYQPCLTG PNQSYRPKSP AASSSSAFLP NAQSSPGPQL PPVSLPGLTT
QPQLPLKEVT SDPSRTPEEE PLNLEGLVAH RVAAYNARLQ GTGQSVGVGH PPLHRLRSSS
LSGGLPDPLP SGSPGKQSDT QPRHLELRNP VFWKLEGWKE ELGVQAREKQ PAEPPAPLRR
RAASNGQYEN QSPEPASPRS PGVRSPVQCV SPELALTIAL NPGGRPKEPH LHSYKEAFEE
MERTSPTSPP PSGVRSPPGL AKTPLSALGL KPHNPASILL HPTGEEDEGK VVTELSEEPR
SYVESVVRTA VAGPRTQDPE PKSFSAPVAQ AYGRETPLRN GTLGGSFVSP SPLSTSSPIL
SADSPPTSHH PGDLSLSNLA QGVAGQPPDS FQSAAPGFGA SSTSVGSFPS GESSDQGPRT
PTQPLLDSGF RSGSLGQPSP SAQRSYQSSS PLPTAGSIYS SPDYSLQQFS SPESQARSQF
SVAGVHTVPG SPQARHRTVG TNTPSSPGFV RRAVNPGMAA PCSPSLSHRQ VMGPPGTGFH
GNTVSSPQSS AATTPGSPSL GRHPGAHQVS SLHGNVSTAP GSPSLGRHPG AHQGNLASSL
HGNAVASPGS PSLGRHLGGS GSVVPGSPSL DQQVAYGGYS TPEDRRPTLS RQSSASGYQA
PSTPSFPVSP AYYPGLSHPA TSPSPDSAAF RQGSPTPALP EKRRMSMGDR AGSLPNYATV
NGKVSSSPVA SGMSSPSGGS AVSFSHTLPD FSKYSMPDNS PETRAKVKFV QDTSKYWYKP
EISREQAIAL LKDQEPGAFI IRDSHSFRGA YGLAMKVSSP PPTIMQQNKK GDMTHELVRH
FLIETSPRGV KLKGCPNEPN FGSLSALVYQ HSVIPLALPC KLVIPHRDPT DESKDSSGPA
NSTSDLLKQG AACNVLFINS VDMESLTGPQ AISKATSETL ATDPTPAATI VHFKVSAQGI
TLTDNQRKLF FRRHYPLNTI TFCDLDPQER KWMKTEGGSP AKLFGFVARK QGSTTDNACH
LFAELDPNQP ASAIVNFVSK VMLSAGQKR
//
