ID   A0A3B3Y6M8_9TELE        Unreviewed;       684 AA.
AC   A0A3B3Y6M8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000022813.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000022813.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the kindlin family.
CC       {ECO:0000256|ARBA:ARBA00008052}.
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DR   RefSeq; XP_014827322.1; XM_014971836.1.
DR   AlphaFoldDB; A0A3B3Y6M8; -.
DR   STRING; 48701.ENSPMEP00000022813; -.
DR   Ensembl; ENSPMET00000011786.1; ENSPMEP00000022813.1; ENSPMEG00000003977.1.
DR   GeneID; 106906508; -.
DR   CTD; 10979; -.
DR   OrthoDB; 5399911at2759; -.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR   CDD; cd17181; FERM_F0_KIND2; 1.
DR   CDD; cd17184; FERM_F1_KIND2; 1.
DR   CDD; cd01237; PH_fermitin; 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; 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:SF11; FERMITIN FAMILY HOMOLOG 2; 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          378..474
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          141..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  78375 MW;  C25DB13DC95551F6 CRC64;
     MALDGIRMPD GCYADGTWEL KMHVTDLHRD VSLRVTGEIH IGGVMLKLVE KLDVKKDWSD
     HALWWEKKKT WLLKTHWTLD KYGIQADARL LFTPQHKLLR LQLPNMKHMK VKVNFSDRVF
     KAVSDICKTF NIRHPEELSL LRKPRDPKKK KKKLEEAEED SLELEGPLLT PGSGSVYSSP
     GLYSKTMTPT YDSRDGSPLS PTSAWFGDSP LSEGNPGILA VSQSIASPDI LVKLYKPQSL
     LDKAKINQGW LDSSRSLMEQ DVKENDVLLL RFKYHSFFDL NPKYDAIRVN QLYEQAKWAI
     LLEEIECTEE EMMMFAALQY HINKLSGMSS DNHMNNSEKE VDEVDAALSD LEITLEGGKT
     SSTLGDITSI PELADYVKVF KPKKLTLKGY KQYWCTFKDI TISCYKSKEE ALGTPAHQMN
     LRGCEVTPDV NISGQKFNIK LLIPVADGMN EIWLRCDTEK QYAHWMAACR LASKGKTMAD
     SSYNLEVQNI LSFLKMQHMN PDPQFIEPIT TDINPECLVS PRYLKKYKNK QPGYVRDLIS
     ARILEAHQNV AQMSLIEAKM RFIQAWQSLP EFGITHFLAK FQGGKKEELI GITYNRLIRM
     DAHTGDAIKT WRFSNMKQWN VNWEIKMVTV EFADEPSLSF ICAEVDCKVV HEFIGGYIFL
     STRAKDQNES LDEEMFYKLT SGWV
//