ID A0A3P8NIK9_ASTCA Unreviewed; 1848 AA.
AC A0A3P8NIK9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tensin 1b {ECO:0000313|Ensembl:ENSACLP00000004645.1};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSACLP00000004645.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000004645.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000004645.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000004645.1}
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; ENSACLT00000004738.1; ENSACLP00000004645.1; ENSACLG00000003009.1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000265100; Chromosome 16.
DR Bgee; ENSACLG00000003009; Expressed in spleen and 8 other cell types or tissues.
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 GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20888; C1_TNS1_v; 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 InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 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; 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; 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 SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..90
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 134..306
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 311..437
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1581..1689
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 107..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1848 AA; 200368 MW; 88C404208C1BBB40 CRC64;
MGGLGWCLAT VFSWAKFFFY CIFPFWKPGK SKNKPEELEA LHSHTFRVKT FKKAKHCSVC
KQTIIQDGFI CRVCRIACHK KCEVKVSSSC VPATNYELAP SSDLPLKHVD TMGSTKSSKS
MESRRRPSRS ASLLQALEES YELDLIYITE RIISVSFPSN VEEQSYAANL REVASMLRSK
HGNNYLLFNL SEKRYDISQL NPKVLDFGWP DHHAPALDKI CSICKAMDTW LSADSHNVVV
IHNKGNRGRT GVVVAAYMHY SNISASADQA LDRFAMKRFY EDKVLPVGQP SQKRYVEYFS
GLLSGHIKIN NKPLFLHHVI MHGIPNFESK GGCRPFLKIY QAMQPIYTSG IYNVQGDSQT
SICITIEPGL LLKGDILLKC YHKRYRSPCR DVIFRVQFHT CAVHDLGIVF GKDELDDTFK
DDRFPEYGKV EFIFSFGPEK IHGQGVDHLE NGPSVSVDYN TQDPLIRWDS YENFNQNCED
TTEGENEVIH TQGPLDGSLY AKVRKKESVD GAVTSNGLPP SAIEHALPAV DHALSVSSDS
GNSTASIKTD RTDEATAAPP ASTVNQTHIP VGEELPSVHQ HAPPAQQSIS PQEKKELEQL
LSGLEGPMHR QAFLSAPASA VGGMLHLVPA QVHVNGHGNI DRETDILDDE LPTSQEGNSV
DSLGTFSSTD GRATPADLYY QSESIINGQD HVPYLERNVP EKPLETVQPQ LGISGKSVTL
PHSDSTPFSG SYMPTQNGSL YRSQSFGAEL KSMPQAPTRT TSSRDAVQRG LNVWQRFGVP
EEPVTEGLTF SPPPTVATMP SHHSLPQFPH RHSASQQEIE QSIETLNLLM LDLEPGRSLV
TKSQSAPLRE NSAVVTTQPS FSQNQTRPSY LPDSTIHTHF SGPMSSHSSP PVKPSTSEPA
PVQRSPSYTS GTASTSTSSQ ASPTVSCQIK TVSTYPPTTL PQSAEASEPQ KSPSASSASP
QPRDSEPDEV FNIEGLVAQR VAEYSARVQS VIPSMTSSQS EHHRSHSLSG VQARVSSLDE
PTAAPRRRIT SEGQNQNGPD DSTSPDVPLR SPIRCVSPEF VNAIAMNPGG RPKEKNMHSY
REAFEELEGG HISPTPTVGG EVFPQTPAFP VSPQTPYFNL CRSPPGLAKT PLSALGLKPH
NPAEILLNQT GSAPRSYVES VAKSAVAGGE PCTSHRSLTP LGDATTKQRS QSPTTTHTLN
PPLSSSSPIQ SSPGDHPVAE SSVSTPSQPT TDSGFRSQPT ESAYPTPTPS YQALNTPTSS
YLDSSSPTSS YLGTATPTPP YLGPSTLLGS YASSDPNPPS SEPVQTTLGH GSPSKQIQTN
IIGSTNNPVL QQRPSINQEV PAMSQQTSPA NGFEVGVSGL SGSPVLGHCP SQGAQSSPVL
NRQAAMGPGP QQSPVLSRQP SLGQPIQSSP VLSRQPSITQ AQGSPVLGRH PSISQMSQRS
PSLDRHPMHS GYTTPDERHG NLSRQSSSSG YQGPPTPSFP ISPAGYQDGG MMGMGLGFRQ
GSPAPGFQPQ LPEKRRMSSG DRPNGALSYG TMNGKMMPTM SGGGNPSYFH TLSDFSRFTM
TDGSPDSRLN VKFVQDTSKF WYKPDISREQ AISLLKDREP GAFVIRDSHS FKGAYGLAMK
VASPPPTVHP NKKGDITNEL VRHFLIESSP KGVKLKGCPN EPYFGCLSAL VYQHAITPLA
LPCKLVIPTT ELTEEVPEVT TANPMAERLK QGAACNVLYI NSVEMESLTG PQAVAKAISE
TLAAASPPTA TIVHFKVSSQ GITLTDNQRK LFFRRHYPTN TVTFCDIDPQ DRKWNKPEGG
TAKLFGFVAR KQGSTTDNVS HLFAELDPDQ PASAIVNFVS KMITSQKR
//
