ID W8B4T3_CERCA Unreviewed; 678 AA.
AC W8B4T3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=SH2B adapter protein 2 {ECO:0000313|EMBL:JAB93587.1};
GN Name=SH2B2 {ECO:0000313|EMBL:JAB93587.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB93587.1};
RN [1] {ECO:0000313|EMBL:JAB93587.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB93587.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- SIMILARITY: Belongs to the SH2B adapter family.
CC {ECO:0000256|ARBA:ARBA00010220}.
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DR EMBL; GAMC01012968; JAB93587.1; -; mRNA.
DR AlphaFoldDB; W8B4T3; -.
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; 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 2: Evidence at transcript level;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 187..297
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 454..552
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 402..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 74136 MW; EFB7D16EDC50355C CRC64;
MGGNSTTNTF TAGGYIGPVS GSSVGSNSGG AVGGDPLPNM TAASSTSYAY GTNWEEFCER
HSRVAAADFA KACINYINGT MPPEEGRKIQ YRNFGQKFAE AFVDHFDAEF CLRRNNIKTG
NGNSLEESGV AEDSPKIFHK AFFRRLSFKG LRKGKNFLFL QTLFHKNSDD LDGSKHSKTK
ISKIIVECRK EGYVHTLSPE SLDQPTGAQK WEKCRLALVK AVGGYMLEFY TPPKATKPRS
GVFCFLISEA RETTALEMPD RENIFVLKAD NNMEYVIEAE SAAEMHSWLA TIRYCMRTPP
TQQLPLDSAD ALATGGTSVG GIMGGITVSN SSTSAMSPSG NSNTTELIAT RSGPSIAIPN
PQYHQTNILG SNGNIGPSDS LPEVALAGSL GATASIANDT TTLEGIPDIP PRPIGPGTRG
EQRLSASSNI EGDCETEADI NVADLTAEMR QYPWFHGTLS RSEAARMVLH SVSAGHGYFL
VRQSETRKGE FVLTFNFQGR AKHLRMTLSE KGQCRVQHLW FPSIQEMLEH FRHNPIPLES
GGTSDVTLTD WVHNKSLLYG GSNDAGNIAE TNGGHQQQQQ QHPSPRHQQE KSLITMNLSV
RLKANEIEIP FLQQPQRPQP HVQFQTQTPQ QNNQQLRAST VSLQSQSQLY SGPRVASISD
LNANEMSTRA VDNQYSFV
//
