ID A0A182N446_9DIPT Unreviewed; 709 AA.
AC A0A182N446;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 2.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR002410-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., 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 dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR002410-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR002410-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; A0A182N446; -.
DR STRING; 7168.A0A182N446; -.
DR EnsemblMetazoa; ADIR002410-RA; ADIR002410-PA; ADIR002410.
DR VEuPathDB; VectorBase:ADIR002410; -.
DR OrthoDB; 5399911at2759; -.
DR Proteomes; UP000075884; 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; cd17095; FERM_F0_kindlins; 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 402..509
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 207..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 80843 MW; 29AC7350F0C51EE6 CRC64;
MIHVGDNTWN LKVYITDLQV QKTLRVRGDL HIGGVMLRLV DPENPKDWSD HALWWPTRNQ
WLTRTKSTLD QVGLHADALL HFTPMHKTLR VQMPDLRYLD CRVDFSIKTF GAVVALCKDL
GIRHPEELSL CKPLEPMHLK KNYADLAKKK IPIEQNGNGR DYIHLPPDTN TFIPVAAHNL
NGSNGSLDGP VNHGPFSCAP VPNSHFSTPK PALQSTPISS PTGTLRHGHG SGFSESSSSI
GDTTDNLAYS PCAPSPEARS RLLKPKSLIE RARMNIGWLD SSLSIMEQGI REFETLCLRF
KYYTFFDLNP KYDQVRINQL YEQAKWQLLN EEMDCTEEEM LMFGALQLQV NKQNEVPQAD
SGIDTSSLDN AADDDVDAAL RELQITLEGP SNGVNAGDIT HIPELTDYLR FLKPKKFTLK
GYKRYWFTYK DLHLHLYKSR EDSRSNSPPQ VSINLRGCEV TPEVNLAQKK FNIKLEVPME
QIINSEMWIR CDNEEQYAKW MAACRLASKG RSLADSSYDS EVASIRSFLS MQKPAQAPAI
NININEMDPN EYLAPRYVKK LKNKAMLRML EAHANVKDLP LIEAKLSYIR AWQSLPEFGV
TLFVIKFDGH KKEELLGVAS NRIMKMDIAT GDHLKTWRYN TMKAWNVNWE IRCMMVQFQN
ETVVFSCLSA DCKVIHEFIG GYIFMSMRSK ETNQTLNEEL FHKLTGGWN
//