ID A0A3L8S7W5_CHLGU Unreviewed; 586 AA.
AC A0A3L8S7W5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
DE Flags: Fragment;
GN ORFNames=DV515_00010933 {ECO:0000313|EMBL:RLV98274.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV98274.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV98274.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV98274.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV98274.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SIMILARITY: Belongs to the kindlin family.
CC {ECO:0000256|ARBA:ARBA00008052}.
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:RLV98274.1}.
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DR EMBL; QUSF01000043; RLV98274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8S7W5; -.
DR STRING; 44316.ENSEGOP00005014251; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13205; FERM_C_fermitin; 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; 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; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 286..382
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RLV98274.1"
SQ SEQUENCE 586 AA; 66335 MW; E59EF48FA0119549 CRC64;
APFSPPDIRH PEELSLLRKP RDPSKKKKKK LDDQCEDDTF ELEGPLITPG SGTDILYIGP
VKGNIYSSPG LYSKTMTPTY DAHDGSPLSP TSAWFGDSAL SEGNPGILAV SQPVTSPESL
AKMYKPQTLL DKAKINQGWL DSSRSLMEQE VKENEALLLR FKYYSFFDLN PKLYEQSKWA
ILLEEIECTE EEMMMFAALQ RGGCVTKILW DPEVTGAPRC DPGLAFQYHI NKLSIMSSEN
HLNHSDKDVD EVDAALSDLE ITLEGGKTST ILGDITSIPE LADYIKVFKP KKLTLKGYKP
YWCTFKDTSI SCYKSKEESN GTPAHQMNLR GCEVTPDVNI SGQKFNIKLL IPVAEGMNEI
WLRCDNETQY ASWMAACRLA SKGKTMADSS YGMEVQNILS FLKMQHLNPD PQLIPEQINT
DINPECLVSP RYLKKYKSKQ ITARILEAHQ NVAQMSLIEA KMRFIQAWQS LPEFGITHFN
ARFQGGKKDE LIGIAYNRLI RMDASTGDAV KTWRFSNMKQ WNVNWEIKMV TVEFADEVRV
SFICTEVDCK VVHEFIGGYI FLSTRAKDQN ESLDEEMFYK LTSGWV
//