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Database: UniProt
Entry: U3KFF0_FICAL
LinkDB: U3KFF0_FICAL
Original site: U3KFF0_FICAL 
ID   U3KFF0_FICAL            Unreviewed;      1565 AA.
AC   U3KFF0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSFALP00000013754.2};
GN   Name=TNS3 {ECO:0000313|Ensembl:ENSFALP00000013754.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000013754.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000013754.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000013754.2}
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; 59894.ENSFALP00000013754; -.
DR   Ensembl; ENSFALT00000013811.2; ENSFALP00000013754.2; ENSFALG00000013179.2.
DR   eggNOG; KOG1930; Eukaryota.
DR   eggNOG; KOG2283; Eukaryota.
DR   GeneTree; ENSGT00940000156328; -.
DR   HOGENOM; CLU_002189_1_0_1; -.
DR   Proteomes; UP000016665; Chromosome 2.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd20889; C1_TNS3_v; 1.
DR   CDD; cd01213; PTB_tensin; 1.
DR   CDD; cd14561; PTP_tensin-3; 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   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; 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; PS50056; TYR_PHOSPHATASE_2; 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   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..68
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          113..285
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          193..274
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          290..415
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          1293..1402
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          472..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1198..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1231..1249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1565 AA;  171549 MW;  63AAA64DAFB170CB CRC64;
     MHKESPRKLQ YRLPQETASR SHTFKNKSFK KSSVCGICKQ VIDSQGISCR VCKYACHRKC
     EEKVVTPCFL PSSYELANNS EVVKNHVTRS NSTSALKNSS FSCDKVLRSA DFDHIMEEGY
     ELDLTYITER IIAVSFPAGC SEETYLHNLQ EVTRMLKSKH GDNYLVLNLS EKRYDLSKLN
     PKIMDVGWPD LHAPLLDKVC TICKAMESWL DNDPQHVVVI HCRGGKGRIG VVISSYMHFT
     NVSASADQAL DRFAMKKFFD DKVSALMQPS QRRYVQFLSG LLSGSVKMNA TPLFLHYVIL
     HGIPNLDAGG ACRPFLKLYQ AMQPVYTSGI YIGSENQSRI CIAIDPAQLL KGDIMMKCYH
     KKYRSATRDV IFRLQFHTGA IQGYSLVFGK EDLDNANKDD RFPDYSKVEL VFSETPEKIQ
     GCEHLLNDHG VIVDYNTSDP LIRWDSYENM SPDGEVLHTQ GPIDGSLYAK VRKKSSSDSN
     IPGDAQGVHV TGSPDHSDHT LSVSSDSGHS SASIRTDKTE ERLVPGGKRG LSPQEKAELD
     QLLSGFGLEE SVSTTKNMTD AQSKYSATHH IVPAQVHLNE VTEMKDRETD ILDDEMPNHD
     LHSVDSIGTL SSSEGQHSTH LGNFSCHKSS QNSLLSDGFG SNAGEEHHNA FAADLGIGVD
     SFYERSFGST EPKSTEQLQQ NPSVSPHPQA YGPSNYSTQT WVRQQQMVTA HQYGFTPENE
     IRVGIHSTVE NLGSVQSQSQ IPDAPTRGSS SRDAVQRGLG SMQGAAEAEE LASADSFKSR
     QMPQRNTNGL DLGQNAGDLA ASPTLDIDQS IEQLNRLILE LDPTFEPIPT RINALTSDRN
     QVNGFSSLDA RMEELNSSSG FHDKLEVTNR NPSGHATGMQ DDDATGKRLR KLSVGQYDND
     VPGEPSYNRC AWMKSPATHQ AVIPGSPVAG GKTKEMTAVH YQDEIDGRIF STIKNGNEDV
     TFTSAFPLSP EKTYVTTSPL CRQQIPSSQK VSSPSELYRT TSESQSYTEA INLSMVMSDS
     TVGTNSPLLR TNMQTDPSFQ RCFASSCTVA SSSPIPGAES SSAAECPWLE SSSKASLSTQ
     FSMGNTRQPG GYVVPSEFSS AVQDVSLLSH FQTPGLQVVT MSNLESSPAE PHQEHDTSSS
     GRAYLSYSTG TRDSSSPREE TQATCTTNAS PSKTLSSSVA SAGDNDFLTQ NFLTVASGHN
     SQNNAVPHYH GGSLHAQPPL PEKKRSSEGE RSFASVSPSS SGFSSPHSGS TISIPFPNVL
     PDFSKMLSPS PVPENTADKH VTVKFVQDTS KFWYKPDISR EQAIAVLKEK EPGSFIVRDS
     HSFRGAYGLA MKVATPPPSV LQLKKVGDLS NELVRHFLIE CTQKGVRLKG CPNEPYFGSL
     TALVYQHSIT PLALPCKLLI PDRDPLEEIA ETSPQTAANS AAELLKQGAA CNVWYLNSVE
     MESLTGYQAV QKALSLTLMQ DPSPVSTVVH FKVSAQGITL TDNQRKLFFR RHYSVNTVLF
     CALDPQDRKW MKDGLSAKVF GFIARKQGSA TDNVCHLFAE HDPEQPASAI VNFVSKVMIG
     SQKKI
//
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