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Database: UniProt
Entry: A0A0V1DIB9_TRIBR
LinkDB: A0A0V1DIB9_TRIBR
Original site: A0A0V1DIB9_TRIBR 
ID   A0A0V1DIB9_TRIBR        Unreviewed;      1154 AA.
AC   A0A0V1DIB9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=Insulin receptor substrate 1 {ECO:0000256|ARBA:ARBA00015710};
DE   AltName: Full=Protein chico {ECO:0000256|ARBA:ARBA00033282};
GN   Name=irs2-b {ECO:0000313|EMBL:KRY60755.1};
GN   ORFNames=T03_15420 {ECO:0000313|EMBL:KRY60755.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY60755.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY60755.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY60755.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Bindings to phosphatidylinositol 3-kinase and SHP2.
CC       {ECO:0000256|ARBA:ARBA00011440}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY60755.1}.
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DR   EMBL; JYDI01000004; KRY60755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1DIB9; -.
DR   STRING; 45882.A0A0V1DIB9; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   CDD; cd01257; PH_IRS; 1.
DR   CDD; cd01204; PTB_IRS; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR039011; IRS.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR019396; TM_Fragile-X-F-assoc.
DR   PANTHER; PTHR10614; INSULIN RECEPTOR SUBSTRATE; 1.
DR   PANTHER; PTHR10614:SF13; INSULIN RECEPTOR SUBSTRATE 1; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF10269; Tmemb_185A; 1.
DR   PRINTS; PR00628; INSULINRSI.
DR   SMART; SM01244; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Differentiation {ECO:0000256|ARBA:ARBA00022943};
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oogenesis {ECO:0000256|ARBA:ARBA00022943};
KW   Receptor {ECO:0000313|EMBL:KRY60755.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        995..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1033..1053
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1083..1103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1124..1147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..116
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          233..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1154 AA;  129774 MW;  E64754E034D88378 CRC64;
     MDPLILFNES NVPDDIIKMG ILRKGKRARK RFFVLHQDSY NGPARLECFD NEKRYRCHAV
     PKLSIPLKTC FNINKKVDSK LKFCIAMYTV DDYLLLGCEN ELDQDAWLHT LLEVLMNTKM
     TGLSDDLRRA NFEYVWQVKV LKNRGLTEKV SKLAGLFRFC LNTCSVYFYK LNTDEEFFEF
     PLVYISNYGH QGNLFFLRVG RSAVTGPGEL WMNTEDVVDA GSMHETMKII LEENHEQRQR
     NMPIEPRGLR SDSQNSTRSN SISVTTTLPP EALMHSDLRS RAISENEKTL QKRCRRRMKI
     KAIVDAIANP TKVLRSHLNY LQHRSHSGVS SKLEYLANLN CYSCGAPPSY SRSASHSPSV
     LHNRSGYHGS ALATSPVIGL SNDSFGSISN SSDFDHFANG LRYSHRQHVG NPSLELISRS
     TIVEESSGGS GTDCVPFCKT SKGILELNDE NSFRPARTLI THCVDVHSSP DCVETFRRMT
     LDSGCVDPVS PRRDADAMSS SYSSEQISDY TPMAPGTTTA LSNAVTDSWR LEDIRPTIGP
     DLVTAVPPLR AYSCGSKPTV RNYGSVKQPS WMRKLQHFSF NDERKRAHSF GNWKSAKLMS
     LRKHSAQQGS DLGDSGGLRQ RSGSFGSDRS SGNSFKHQLP GRIFDSKFSS GSEDLVEIDF
     GAFPYGRSNS GSFGSGDSLN RSRASSAGTA SIYRQSWSPK IEQISEQELS PSAKLIQDLI
     FTRRCRPSLE RLAEYVPMSP PVANVNDDTV SGKGSTSMFG SAEGDHVDVN DVDEDDDETD
     IMRVTREKKG LGSFRIRPVS DEITFSPDVD SSMDILQGVD RMMHSDISSF GRGNSAANAT
     TVPLAAASLE QRLRFQRPMS SCKWSAAPRC SIRRRHSIGD PCGSIYEELK RRKKERFFHS
     DMNFITKFPL SECCKSISLL KRIGRRSLPA DFSFQCFSRS PYSSHADKSR LKMVTTHNSN
     NSNSGNTNTI NNAEDDYLML EPVSQFNLGT VVQRLFFLIS MSAIHRALFL WSCIMAFVII
     AVMRLDGRIS WHWSVVFTPL WILDLVALFY TLLSCVRQVH LLRACSIGFA QIASDGYCKR
     RNVSFLLVIL FKLCFLSLLS VKLEQQQHQH SAVGKFSTGE SIKFWHVMLP FWASVSIALA
     EITYRLYHIY KCEM
//
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