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Database: UniProt
Entry: A0A087Y1A4_POEFO
LinkDB: A0A087Y1A4_POEFO
Original site: A0A087Y1A4_POEFO 
ID   A0A087Y1A4_POEFO        Unreviewed;       689 AA.
AC   A0A087Y1A4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=SH2B adaptor protein 2 {ECO:0000313|Ensembl:ENSPFOP00000011807.2};
GN   Name=SH2B2 {ECO:0000313|Ensembl:ENSPFOP00000011807.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011807.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000011807.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SH2B adapter family.
CC       {ECO:0000256|ARBA:ARBA00010220}.
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DR   EMBL; AYCK01003516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007549581.1; XM_007549519.2.
DR   AlphaFoldDB; A0A087Y1A4; -.
DR   STRING; 48698.ENSPFOP00000011807; -.
DR   Ensembl; ENSPFOT00000011824.2; ENSPFOP00000011807.2; ENSPFOG00000011778.2.
DR   GeneID; 103136322; -.
DR   KEGG; pfor:103136322; -.
DR   CTD; 10603; -.
DR   eggNOG; ENOG502QT43; Eukaryota.
DR   GeneTree; ENSGT00950000183191; -.
DR   OMA; YHRMEGT; -.
DR   OrthoDB; 2995825at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01231; PH_SH2B_family; 1.
DR   CDD; cd10411; SH2_SH2B2; 1.
DR   Gene3D; 6.10.140.110; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR015012; Phe_ZIP.
DR   InterPro; IPR036290; Phe_ZIP_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR030523; SH2B.
DR   InterPro; IPR035058; SH2B2_SH2.
DR   PANTHER; PTHR10872; SH2B ADAPTER PROTEIN; 1.
DR   PANTHER; PTHR10872:SF4; SH2B ADAPTER PROTEIN 2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF08916; Phe_ZIP; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF109805; Phenylalanine zipper; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}.
FT   DOMAIN          250..364
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          473..571
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          122..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  73899 MW;  DB121A48A70F728A CRC64;
     MNGAVLPGSP ELSSSCPLPD WREFCELHAR ASAADFADKF QRFLSENPCY DSPGADASFS
     QHFANHFLEC FSAALTQAKE KQASSPGEDG CNAATKYSIV PFLGIQGCPL TYGHDLYQRR
     KDTGASSESL DSMDSGGGGM DGGGGGGSTS SRGPQNHKMS VLGQSRSSED VSVSHPKARF
     KKGFSLRNMS LCVVDGVKEM WHRRASPEPD APSGARRANG AGGEAGGGEK WSQKLRLPRS
     SQGHKAELLE IQREGALRYM VADDTNCMGA AQWQKCRLLL RKTKREDGGE KFLLEFYVPP
     KCSKPKVSIP LSAIVEVRTT MPLEMPDKDN TFVLKVENGG EYILETIDSL QKNSWVADIQ
     DCIDPGDSGD DIELASCPHG QASKDCSMVA SCSCELLSEG VYRAPERSCP TAADHYSAPS
     VRCREPPFTQ HPSHMPLERF LQSPEAQSSN ASAGGGEGTK EPEGDASLAG YPWFHGTLSR
     VRAAQLVLAG GARSHGLFVI RQSETRPGEY VLTFNFQGKA KHLRLSVNEN GQCHVHHLWF
     HTVTDMLRHF HAHPIPLESG GSADITLRSY VQVQRSSAAD ATVPPVFTPP RDASCRADPV
     QPALHPPGTA APAGPSSDGP LSSSTSSSPT ALPSLSRSDP GTGLGGGGLQ SRSNSSERLL
     EASSGASEDY HDADGTRRAR AVENQYSFY
//
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