ID A0A493TZG1_ANAPP Unreviewed; 924 AA.
AC A0A493TZG1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=PH domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000031184.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000031184.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000031184.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSAPLT00000023638.1; ENSAPLP00000031184.1; ENSAPLG00000030420.1.
DR GeneTree; ENSGT00940000157340; -.
DR Proteomes; UP000016666; Chromosome 1.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR CDD; cd13275; PH_M-RIP; 1.
DR CDD; cd11914; SH3_BAIAP2L2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR039597; M-RIP_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR035593; Pinkbar_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR17271; PLECKSTRIN HOMOLOGY PH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR17271:SF10; TRIO AND F-ACTIN-BINDING PROTEIN; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 11..107
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 582..661
FT /note="IMD"
FT /evidence="ECO:0000259|PROSITE:PS51338"
FT DOMAIN 749..812
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 131..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 137..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 104223 MW; CD69B21A2E030861 CRC64;
MPSRWREPDL LNFKKGWMSI LDEPGEWKKH WFVLTDSSLR YYRDSNAEEA DDLDGEIDLR
SCTDVTEFAV QRNYGFQIHT KDAIFTLSAM TSGIRRNWIE ALRKNVRPVS APDVTKLSDC
NKENALRNCV PARGSLRAEE QQQQQQRPGS EGSTKSSPWK ADGQRHAFDY VELSPLQQDP
PSQGSPPRTR GSLRGSERAP KHHEDLERDL ALRSEERRRW FESPDSGVPN ADGLGGDSSR
KAGEPDLPPS PLSEEQRARL NEEIEKKWLE LERLPLKDSR RVPLTALLNQ GKGNQGGDLN
EALRKEVQSL RAQLESCRAK NEATKPQGDS HVPRGYISQE ACERSLAEME SSHQQVMEEL
QRHHQRELER LRQEKERLLA EEAAATAAAI EALKKAHREE MNKELGRTRS FQQCGSSSDA
LQKQHQLDVD SLKRELQVLS EQYSQKCLEI GQLTEKAEER EQTLQRCQQE GKQLLRKNQE
LQTRLSDEIG KLRSFISSRC SGDRSQNNER SSCELEVRGW QGQTLKEIWA RRGTTGRPXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XFPLVGQENV MRLRSEMQAF VSESQREAEL
EEKRRYRFLA EKHQILYNTL LQFYSRAQGM IQNKAPQWKE QLEASRNPSN SHAQGLLAAS
HSQGYLSGRS TPTHLEMLQK PLGDFTSSMS GNRSSIFSQE PEMKMSPQPE LSRRPLQRTP
SASLLPTGRI SRSGSFGEAS SSSEGRRKSG AVRVQAIVPH TTGTNRTLLR FDPGDVITVL
MPEAQNGWLY GKLEGSSTCG WFPEAYVKPL DDVRDVEEPT TRSFPLRSSH SMDDILDRPS
VSSSNTHWPA AAQAAVPNPP PPPLAASSHQ SGLGTLAGSG SKVSAGWRVR SRARLSIRAD
FQPFLRRPVE KDDTNTYICA LVLS
//