ID   A0A182P556_9DIPT        Unreviewed;       664 AA.
AC   A0A182P556;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
OS   Anopheles epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI002044-PA, ECO:0000313|Proteomes:UP000075885};
RN   [1] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AEPI002044-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI002044-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the kindlin family.
CC       {ECO:0000256|ARBA:ARBA00008052}.
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DR   AlphaFoldDB; A0A182P556; -.
DR   STRING; 199890.A0A182P556; -.
DR   EnsemblMetazoa; AEPI002044-RA; AEPI002044-PA; AEPI002044.
DR   VEuPathDB; VectorBase:AEPI002044; -.
DR   OrthoDB; 5399911at2759; -.
DR   Proteomes; UP000075885; Unassembled WGS sequence.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13205; FERM_C_fermitin; 1.
DR   CDD; cd17096; FERM_F1_kindlins; 1.
DR   CDD; cd01237; PH_fermitin; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR037843; Kindlin/fermitin.
DR   InterPro; IPR040790; Kindlin_2_N.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR037837; PH_Kindlin/fermitin.
DR   PANTHER; PTHR16160; FERMITIN 2-RELATED; 1.
DR   PANTHER; PTHR16160:SF13; FERMITIN 2-RELATED; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF18124; Kindlin_2_N; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889}.
FT   DOMAIN          357..464
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          164..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  75548 MW;  79E22A44BDF0713D CRC64;
     NPKDWSDHAL WWPARNQWLT RTKSTLDQVG LHADALLHFT PMHKTLRVQM PDLRYLDCRV
     DFSIKTFGAV VALCKDLGIR HPEELSLCKP LEPMHLKKNY ADLAKKKIPI EQNGNGRDYI
     HLPPDTNTFI PVANLNGSNG SLDGPVNHGP FSCAPVPNTH FSTPKPALQS TPISSPTGTL
     RHGNGSGFSE SSSSIGDGME NLAYSPYAPS PEARSRLLKP KSLVERARMN IGWLDSSLSI
     MEQGIREFET LCLRFKYYTF FDLNPKYDQV RINQLYEQAK WQLLNEEIDC TEEEMLMFGA
     LQLQVNKQNE VPQADSGIDT SSLDNAADDD VDAALRELQI TLEGPSNGVN AGDITHIPEL
     TDYLRFLKPK KFTLKGYKRY WFTYKDLHLH LYKSREDSRS NGPPQVTINL RGCEVTPEVN
     LSQKKFNIKL EVPLDQSINS EMWIRCDNEE QYAKWMAACR LASKGRSLAD SSYDSEVASI
     RSFLSMQKPA QAPAININPG EIDPNEYLAP RYVKKLKNKA MIRMLEAHAN VKDLPLIEAK
     LSYIRAWQSL PEFGVTLFVI KFDGHKKEEL LGVASNRIMK MDIATGDHLK TWRYNTMKAW
     NVNWEIRCMM VQFQNETVVF SCLSADCKVI HEFIGGYIFM SMRSKETNQT LNEELFHKLT
     GGWN
//