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
//