ID A0A1J1I134_9DIPT Unreviewed; 1709 AA.
AC A0A1J1I134;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=CLUMA_CG005661, isoform B {ECO:0000313|EMBL:CRK92081.1};
GN Name=putative Tensin-1 {ECO:0000313|EMBL:CRK92081.1};
GN ORFNames=CLUMA_CG005661 {ECO:0000313|EMBL:CRK92081.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK92081.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK92081.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR EMBL; CVRI01000023; CRK92081.1; -; Genomic_DNA.
DR Proteomes; UP000183832; Unassembled WGS sequence.
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:0051179; P:localization; IEA:UniProt.
DR CDD; cd01213; PTB_tensin; 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; 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; IPR033929; Tensin_PTB.
DR PANTHER; PTHR45734:SF10; BLISTERY, ISOFORM A; 1.
DR PANTHER; PTHR45734; TENSIN; 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; SM00252; SH2; 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; PS50001; SH2; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
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:UP000183832};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 193..234
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 443..573
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1433..1537
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1709 AA; 195424 MW; 47A267CB654A0AB7 CRC64;
MPWNCLCSSS KKSKKSKYNE NIKNHNDVPE NTEPEKKRKP KFYTNLRLDQ CEKNPKTNNS
SSLDSQFDQK SINELNEHLY DSYDTLPNLN KNIVNVPENN KNYLNVNQQQ EKQRSMGKID
DDDNILRPKH LILCLSNENL PFIDSDSPGC SHYNDRIIEM MPRNLLMSSS MERQNNSASE
WEKLHHMQKT FPTHKYIEID VMDAQICQKC HKHLSFKKTY KCTLCDFICH QICAVDKSGS
YEDRQQQLER NELHNRPKTP TKNQLCYVTE RILAAVLPTK DTSAKINDLF LYDENGNRRG
DKHETDLLQM LEQKHGKNFR LFDLESCIPT ISLEKLCELC KHIESWLNSG HNKIVVLQDR
ESFQRVGASV AAYLHYQKIC STNLAPYSIR SNSSDPSRNI QDLDEYSMQK FLDDIVGPIT
EPALKRYLEY FIGLLSGEIK INSQPLYLRF IKMESPPCMH HKISHHENEW SSFIKVFEGE
KFVFISDIYI MPISTKQFIY EIKNPLNLRG DIFVHFFQIH NKSRQTELIS TVQFHTCAIT
RNEVEFHKSD ISFPRSDEKF PTDHKITLIF NKNADPDNSN RSNSDVLMFQ NPLIRKEPIS
NFSSIADLSQ YAQHTHGPVD GSLYATIAKA AAANNSNHAD NELTVQNIQT IETRLNTPPT
SKNSRILSTI LEWDNIRNGG ENGGVGEHNN GGGGYMNTAS LRTRQEQPRS FVKSPLMRSY
DSGIYSHEVT NKNNTSSALS WHDGATSPTT ANNCHVELDN LLSEMLLTVE TLPDISYSNS
NTTRNKQIEV FSMKRSNANE RTSPHRTTFE SNTINTNANN QEFKRSHVQH MKNYNLDTFG
YSKNNQDIGE TSSITTTTLT PTESRCNTPA MSDHQGMFKA YQHHDELYYD TDTQMQLHGG
RQRQFQLQHI DNTSRKEYEK QTENLLQSSS QSNSYMEVLR SENRSGDRPD SNIPYHAREY
SKPFSYGIPG EGRMMKMQTG LSSPSMVRKA LNVNGTSGRK TPVHEFEERA KYGRYVENKY
TIGDKTPENN LSVFDNNKEF DYRNRSENQR YKDGASFSIE NSDVESAHYF EPLRRSNTMD
GSFGRSGYAS DGGSSQTWLQ VQQQRLRAKR AQRPKEVFDF TDGASRRSQT LSPVRNYNTL
AVAKEPKFVT IKRTTEQVVS KPYKNDYLES NPFDYHNRTA SHSRSYNEKF ATINNMARRN
MPITSTPYEA MDHINNNTME STSEMDALDN ILESIAFENF TTNIHLSEMV NGVAKESKVN
LTSNDNINIS NKTDTLNRFF DNLINFNREC EKANIRKSES SSDHSSSPDH QNNNNKNNFN
GRVPYPQTRN ESVSSYRSET ETEVSRPETP AFPVTPRTPI HFGSTSTLPP KSPTLQRRDL
SNRIHEVANV NETVSTYTSR RNSSNSAISN ANSEPFEIAP HHVKFARDSS RFWYKPALTR
EEAINLLRNA QPGTFVVRDS TTFANAFGLV VRVSQPPPGT KGQGGDELVR HFLVEPTVRG
VRLKGCSNEP VFSSLSALIY QHSVTPLALP CRLILPERDI QYRDNYQTSG QKQIVSQGAA
CNVLYLFSVD TESLTGPQAV RKAIRLLFER RPLPTPTEVH FKVASQGITL TDNSRQLFFR
KHYPVNSVTF FGLDPDDHRW SVQVTNEEIP VQNQHIFAFI AKKSSSSSDN QCHIFCELEA
RQPASAIVSF AQKVLLDEAT RQQHAPAQI
//
