ID A0A2A3EST4_APICC Unreviewed; 604 AA.
AC A0A2A3EST4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE SubName: Full=SH2B adapter protein {ECO:0000313|EMBL:PBC34199.1};
GN ORFNames=APICC_03130 {ECO:0000313|EMBL:PBC34199.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC34199.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC34199.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC34199.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH2B adapter family.
CC {ECO:0000256|ARBA:ARBA00010220}.
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DR EMBL; KZ288192; PBC34199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3EST4; -.
DR STRING; 94128.A0A2A3EST4; -.
DR Proteomes; UP000242457; 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; cd10346; SH2_SH2B_family; 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; IPR035057; SH2B1_SH2.
DR PANTHER; PTHR10872:SF2; LNK, ISOFORM D; 1.
DR PANTHER; PTHR10872; SH2B ADAPTER PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF08916; Phe_ZIP; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
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:UP000242457};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 218..324
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 427..525
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 188..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 67429 MW; F3A516F57A1E9529 CRC64;
MSVYTITAAT PTTSTIISTT TATTTTAVTV TTTATPTTTA PAVAVSPEAA PGWIEFCERH
ARASASDFAK AFCTYVSLNL PESARLNLSH HDFLKKFVES FCEHFENEYL RRTVRSPSLY
DTRHSATNDR DINAISQNNN APIRISSHEE FSDYSEHDGD AISPKPSHKP FFRRLSFKGL
KKGKSLFHKQ QSDEVELSHS EHRRDKHSKA KLSKIVVECR KEGIVNSLMG ENIDGTQKWE
KSRLALIKAI GGYMLEFYSP PKAVKPRSGV FCSAITEARE TTALEMPDHE NTFVLKTQNM
EFVIEAHDSN DMRSWLATIK YCMRTVQQNS INPNSGVEAT GESLGHASLA ISNEGDRLRT
NSASKSSRST SHEHGDEIGG NPPEIPPRLR IRSNSNLELC SSQQDIEQLN VNDGELDLSS
SLREYPWFHG TLPRSDAAQL VLHSAANGHG VFLVRQSETR KGEFVLTFNF QGRAKHLRMT
LNDQGHCRVQ HLCFPAIYDM LEHFRQNAIP LESGGTADVT LTEFVVANHA IRSAHHNMSG
INQQQLQERR PPVAPEPREV RTYGGSIRTR TESLERLEQQ NTITEQQSSS STSGRAIQNT
YSFL
//