ID   A0A2Y9ESV1_PHYMC        Unreviewed;       549 AA.
AC   A0A2Y9ESV1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha isoform X3 {ECO:0000313|RefSeq:XP_023985107.1};
GN   Name=PIK3R1 {ECO:0000313|RefSeq:XP_023985107.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023985107.1};
RN   [1] {ECO:0000313|RefSeq:XP_023985107.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023985107.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009442}.
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DR   RefSeq; XP_007108388.1; XM_007108326.1.
DR   RefSeq; XP_023985107.1; XM_024129339.3.
DR   Proteomes; UP000248484; Chromosome 8.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd12924; iSH2_PIK3R1; 1.
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; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   InterPro; IPR044124; ISH2_PIK3R1.
DR   InterPro; IPR032498; PI3K_P85_iSH2.
DR   InterPro; IPR035020; PI3kinase_P85_cSH2.
DR   InterPro; IPR035022; PI3kinase_P85_nSH2.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
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; PF00620; RhoGAP; 1.
DR   Pfam; PF00017; SH2; 2.
DR   PRINTS; PR00678; PI3KINASEP85.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00252; SH2; 2.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50001; SH2; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016}.
SQ   SEQUENCE   549 AA;  64338 MW;  F8FD58E5D1B9D115 CRC64;
     MIDVHVLADA FKRYLLDLPN PVIPVAIYNE MVSLAPEVQS SEDYIQLLKK LIRSPSIPHQ
     YWLTLQYLLK HFFKLSQTSS KNLLNARVLS ELFSPLLFRF PAASSENTEH LIKVIEILIS
     TEWNERQPAP ALPPKPPKPT TVANNGMNNN MSLQDAEWYW GDISREEVNE KLRDTADGTF
     LVRDASTKMH GDYTLTLRKG GNNKLIKIFH RDGKYGFSDP LTFNSVVELI NHYRNESLAQ
     YNPKLDVKLL YPVSKYQQDQ VVKEDNIEAV GKKLHEYNTQ FQEKSREYDR LYEDYTRTSQ
     EIQMKRTAIE AFNETIKIFE EQCQTQERYS KEYIEKFKRE GNEKEIQRIM HNYEKLKSRI
     SEIVDSRRRL EEDLKKQAAE YREIDKRMNS IKPDLIQLRK TRDQYLMWLT QKGVRQKKLN
     EWLGNENTED QYSLVEDDED LPHHDEKTWN VGSSNRNKAE NLLRGKRDGT FLVRESSKQG
     CYACSVVVDG EVKHCVINKT ATGYGFAEPY NLYSSLKELV LHYQHTSLVQ HNDSLNVTLA
     YPVYAQQRR
//