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Database: UniProt
Entry: A0A401NU71_SCYTO
LinkDB: A0A401NU71_SCYTO
Original site: A0A401NU71_SCYTO 
ID   A0A401NU71_SCYTO        Unreviewed;       773 AA.
AC   A0A401NU71;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha {ECO:0008006|Google:ProtNLM};
GN   ORFNames=scyTo_0007532 {ECO:0000313|EMBL:GCB64407.1};
OS   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB64407.1, ECO:0000313|Proteomes:UP000288216};
RN   [1] {ECO:0000313|EMBL:GCB64407.1, ECO:0000313|Proteomes:UP000288216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009442}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCB64407.1}.
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DR   EMBL; BFAA01002749; GCB64407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401NU71; -.
DR   STRING; 75743.A0A401NU71; -.
DR   OMA; GNENTEX; -.
DR   Proteomes; UP000288216; Unassembled WGS sequence.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd12924; iSH2_PIK3R1; 1.
DR   CDD; cd04388; RhoGAP_p85; 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   Gene3D; 2.30.30.40; SH3 Domains; 1.
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   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
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   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          46..122
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          155..344
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          380..475
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          673..767
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          123..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          496..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          561..609
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        127..144
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  88768 MW;  2AFFF5EB2CA7D8E8 CRC64;
     MRCWHQVGTA LRPIISDTAY FEGNGTKLFK SSLTKQGLST IGKMSADGYQ YRALYEYKKE
     REEDIDLHTG DILIVTKNTL LALGFSEGAE AKPDEIGWLT GLNETTQERG DFPGTYVEFH
     GFRKISPPTP KPRPPRPLPV APNPLRPEDS DLQASVLPDL TEQFSPPDIA PTLLVKLVEA
     IEKTGIENTN LYRTSGSYGS TELKQLLDYD ATPMDIEQLD LQSLADVLRQ YLQELPNPVI
     PASIHSDLVS IAQEVLNTEE CAQLLRRAIR SHNVPHQYWL TLHYLIKHFC KLCQSSGKNN
     LSARTLAEIF SPLLFRQQAA NSDTNPEYHI KIIEVLIASE CQETQPTPAS APALPPKPPK
     PTPVTNNGIN SNMSLQDAEW YWGDISREEV NEKLRDTADG TFLVRDASTK MHGDYTLTLR
     KGGNNKLIKI FHRDGKYGFS DPLTFNSVVE LINHYRHESL AQYNPKLDVK LLYPVSKFQQ
     DQVVKEDNID AVGKKLHEYH TQYQEKSREY DRLYEECTRT SQEIQMKRTA IEAFNETIKI
     FEEQCQTQER YSKEYIEKFR REGNEKEIQR IMVNYEKLKS RISEIVDSKR RLEEDLKKQA
     ADYREIDKRM NSIKPDLIQL RKTRDQYLTW LTQKGVRPKK INEWLGIKNE NAEDQYSMVD
     DDEDLPHHDD RTWNVGSINR TRAESLLRGK RDGTFLVRES SKPGCYACSV VVDGDVKHCV
     INKTPTGYGF AEPYNLYNSL RELVLHYQHT SLVQHNDSLN VTLAHPVYAN QRR
//
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