ID G1NGF9_MELGA Unreviewed; 1670 AA.
AC G1NGF9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMGAP00000012171.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000012171.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000012171.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000012171.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; ENSMGAT00000013058.3; ENSMGAP00000012171.3; ENSMGAG00000011587.3.
DR GeneTree; ENSGT00940000155400; -.
DR InParanoid; G1NGF9; -.
DR TreeFam; TF315996; -.
DR Proteomes; UP000001645; Chromosome 7.
DR Bgee; ENSMGAG00000011587; Expressed in gizzard and 17 other cell types or tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14560; PTP_tensin-1; 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; IPR035892; C2_domain_sf.
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; 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; 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; 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.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 71..243
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 248..374
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1398..1507
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1670 AA; 179390 MW; 51738C7AF6A2B717 CRC64;
MGMLRLRQDL EEEEGEEGCG KEAATPCSPA VNYELPSPGQ SITKQVDTLD ATRSPRGGQA
HRKTARSMSV TAAMESSCEL DLVYITERII AVSYPSTAEE QSFRSNLREV AHMLKSKHGD
NYVLFNLSER RHDISKLHPK VLDFGWPDLH TPALEKICSI CKAMDTWLNA AAHNVVVLHN
KGNRGRLGVV VAAYMHYSNI SASADQALDR FAMKRFYEDK VVPVGQPSQK RYIHYFSGLL
SGSIKMNNKP LFLHHVIMHG IPNFESKGGC RPFLKIYQAM QPVYTSGIYN VQGDSQTGIC
ITIEPGLLLK GDILLKCYHK KFRSPTRDVI FRVQFHTCAV HDLDIVFGKE DLDEAFRDER
FPEYGKVEFV FSYGPEKIQG MEHLENGPSV SVDYNTSDPL IRWDSYENFN IQREDSAEGA
WAEPTLPGKH LEKEVGHTQG PLDGSLYAKV KKKDSLHGSI GAVNTARLPL SAAPNHVEHT
LSVSSDSGNS TASTKTDRTD EPGAPGAPGG HTVLSPEEKR ELDRLLVGFG LESAAPMHNH
APGPAPARLP AGSGRHVVPA QVHVNGAGTP LLAERETDIL DDELPNQDGH SVGSLGTLSS
LDGTTTASEA GFHEAPRVGS LSSLPNGPAS YNGAEKMLKE GLYEAEPLSN GAYPYSNQNT
LMGHHLRDPL AHLRPSASAQ EHLAGYSQRQ PASASPAWLQ PPVPQPYLYG YDLPSAHRSQ
SFPAVGTAKY DANPALPQAP ARSTSSREAV QRGLNSWQQQ GGSRPPSQLH DGGLESHSPS
LSSCSPQPSP LQPMPPHSHS MPEFPRAPSR REIEQSIEAL DVLMLDLAPS VHKSQSVPSA
VARQDKPAAT LSSLSAQPLS GHYAQPAPQV VQPRSFGTSV GTDPLAKAYS PGPLVPAARS
TVEPDYTVHE YRETYTPYSY QPEPRSYGSA PASILPLSAS YSPAGSQQLL VSSPPSPTAP
AQSQLPHKGL ESYEDLSRSG EEPLNLEGLV AHRVAVRSPP GLAKTPLSAL GLKPHNPADI
LLHPVGELEG EAGADSEEEP RSYVESVART ATTGRAGNLP AAQPVGLEVP ARNGAFGNSF
TVPSPISTSS PIHSIDGASL RSYPSEGSPH GTVTPPHAVA EPAYRSPIVS QTPSAHSSYQ
TSSPSSFQAG TLGSPYASPD YPDGRAGFQP DPQVRQQPQV SVVGVHALPG SPRTLHRTVA
TNTPPSPGFG RRAANPAVAS TPGSPGLGRH AMSPHAPPGS PSLARHQMAA VPPGSPVYGY
SSPEERRPTL SRQSSASGYQ PPSTPSFPVS PAYYPGTSTP HSSSPDSAAY RQGSPTPQPA
LPEKRRVSAG ERSNSLPNYA TVNGKASSPL SSGMSSPSSG STVAFSHTLP DFSKFSMPDI
SPETRANVKF VQDTSKYWYK PDISREQAIA LLKDREPGAF IIRDSHSFRG AYGLAMKVAS
PPPTVMQQNK KGDITNELVR HFLIETSPRG VKLKGCPNEP NFGCLSALVY QHSIMPLALP
CKLVIPDRDP MEEKKDVAST TNSATDLLKQ GAACNVLFIN SVEMESLTGP QAISKAVAET
LVADPTPNAT IVHFKVSAQG ITLTDNQRKL FFRRHYPLNT VTFCDLDPQE RKWTKTDGSG
PAKLFGFVAR KQGSTTDNVC HLFAELDPDQ PAAAIVNFVS RVMLGSGQKR
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