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Database: UniProt
Entry: A0A2Y9QLV2_TRIMA
LinkDB: A0A2Y9QLV2_TRIMA
Original site: A0A2Y9QLV2_TRIMA 
ID   A0A2Y9QLV2_TRIMA        Unreviewed;      1059 AA.
AC   A0A2Y9QLV2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Tensin-3 {ECO:0000313|RefSeq:XP_023580218.1};
GN   Name=LOC101345078 {ECO:0000313|RefSeq:XP_023580218.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023580218.1};
RN   [1] {ECO:0000313|RefSeq:XP_023580218.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000256|ARBA:ARBA00007881}.
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DR   RefSeq; XP_023580218.1; XM_023724450.1.
DR   AlphaFoldDB; A0A2Y9QLV2; -.
DR   STRING; 127582.A0A2Y9QLV2; -.
DR   KEGG; tmu:101345078; -.
DR   InParanoid; A0A2Y9QLV2; -.
DR   OrthoDB; 3439226at2759; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14561; PTP_tensin-3; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR45734; TENSIN; 1.
DR   PANTHER; PTHR45734:SF5; TENSIN-3; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00404; PTPc_motif; 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   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          86..133
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          164..336
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          269..325
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          341..467
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   REGION          148..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1059 AA;  115688 MW;  2751AD550A9B2D63 CRC64;
     MQKLVEPQGK IDKCINIIRY FITPFPIVNR TSRQKLSKAI EDLNNIIKQL DPIDICRTFD
     PIGAAFTFFS SAHGTVTEPE ELATSPHSFK KKAFKKSKVC GVCKQIIDGQ GISCRVCKYS
     CHKKCKAKVA VPCCVPVPWE QASGSSSPTA PLCQHRNSRL TAPNPTMEDS QELDLTYITE
     RIIAVSFPAS SSEESYLHNL QEVTRMLKSK HGDNYLVLNL SEKRYDLTKL NPKTMDVGWP
     DLHAPPLDKM CTICKAQESW LNSDPQHVVV IHCRGGKGRI GMIISSYTHF TNVSASADQA
     LDRFAMKKFY DDKVSALMQP SQKRYVQFLS GLLSGSVKMN ASPLFLHFVI LHGIPNFDTG
     GVCRPFLKLY QAMQPVYTSG IYTVSPENQS RVCIAIEPAQ LLKGDIMVKC YHKKYRSATR
     DIIFRLQFHT GAVQGYGLVF GKEDLDNASK DDRFPDYGKI ELVFSATPEK IQGSEHLHND
     HGVIVDYNTA DPLIRWDSYE NLGADGEVLH TQGPVDGSLY AKVRKKSTSD PSIPGGPQAV
     LATHSPDHSD HTLSVSSDSG HSTASVRTDK TEERLAPGAK RGLSPQEKAE LDQLLSGFGL
     EESENSFKDM TDAQSKYSGT RHVVPAQVHV NGDAKLRDRE TDILDDEMPN HDLHSVDSLG
     TLSSSEGQPL AHHGAFTCHK SSQNSLLSDG FGSNTGEDPP GSLGPDLGMS VELLYERSFG
     NREPRQPPAL LKKPSVSAQT QTYGQSGYST QTWVRQQQMV AAHQYSFSPD GEARLVSRGT
     AENAGLIPAQ PRVPVNPTRG ASSRVVVQRG VGSGPNPPET QLPPPSKAFK PVFANENAMN
     GVDLELNPVL SPGSPTLDID QSIEQLNRLI LELDPTFEPL PTHMNTLGSQ TNGAATPDGV
     GSRLRASGRL QDPGEGPSRM PGRQGPIGDD PLGGRLRKLS LGQYDNDAGG QPSFSKCNWG
     KTTTVDQDPS MASFLNSADT KETVITSYPS DIDVINGRIF SPTKNGSESA PSTPAFPVSP
     ETPYVKTPPH YPPFNPLEPK MSSPVSLYKG AHGKKFTHF
//
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