ID A0A093HS44_STRCA Unreviewed; 434 AA.
AC A0A093HS44;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphatidylinositol 3-kinase regulatory subunit gamma {ECO:0000313|EMBL:KFV84456.1};
DE Flags: Fragment;
GN ORFNames=N308_02888 {ECO:0000313|EMBL:KFV84456.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV84456.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV84456.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV84456.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC {ECO:0000256|ARBA:ARBA00009442}.
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DR EMBL; KL206638; KFV84456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HS44; -.
DR STRING; 441894.ENSSCUP00000016848; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035020; PI3kinase_P85_cSH2.
DR InterPro; IPR035022; PI3kinase_P85_nSH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10155:SF10; PI3K21B, ISOFORM B; 1.
DR Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00678; PI3KINASEP85.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KFV84456.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Transferase {ECO:0000313|EMBL:KFV84456.1}.
FT DOMAIN 37..132
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 330..424
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..180
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV84456.1"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:KFV84456.1"
SQ SEQUENCE 434 AA; 51027 MW; CCB8CC791A49B9A9 CRC64;
IEMDPPALPP KPPKPMAPVN TNGIKDNSSF SLQEAEWYWG DISREEVNDK LRDMPDGTFL
VRDASTKMQG DYTLTLRKGG NNKLIKIYHR DGKYGFSDPL TFNSVVELIN HYRNESLAQY
NPKLDVKLMY PVSRYQQDQL VKEDNIDAVG KKLQEYHAQY QEKSKEYDKL YEEYTRTSQE
IQMKRTAIEA FNETIKIFEE QCHSQERYSK EYIERFRREG NDKEIERIMM NYEKLKSRLG
EIHDSKMRLE QDLKKQALDN RETDKKMNSI KPDLIQLRKI RDQYLVWLNH KGVRQKRIND
WLGIKNENID DTYFVNEEDE NLPHHDEKTW FVGDLNRIQA EDLLCGKPDG AFLIRESSKK
GCYACSVVAD GEVKHCVIYS TPRGYGFAEP YNLYSTLKDL VLHYQQTSLV QHNDSLNVRL
AYPVYAQMPP SLCR
//
