ID A0A2K5I3Y9_COLAP Unreviewed; 677 AA.
AC A0A2K5I3Y9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000011261.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000011261.1}
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_011796398.1; XM_011941008.1.
DR AlphaFoldDB; A0A2K5I3Y9; -.
DR STRING; 336983.ENSCANP00000011261; -.
DR Ensembl; ENSCANT00000034158.1; ENSCANP00000011261.1; ENSCANG00000029047.1.
DR GeneID; 105511005; -.
DR KEGG; cang:105511005; -.
DR CTD; 55612; -.
DR OMA; GMFFCAP; -.
DR OrthoDB; 5399911at2759; -.
DR Proteomes; UP000233080; Unplaced.
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; cd17180; FERM_F0_KIND1; 1.
DR CDD; cd17183; FERM_F1_KIND1; 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:SF12; FERMITIN FAMILY HOMOLOG 1; 1.
DR Pfam; PF00373; FERM_M; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT DOMAIN 377..473
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 77299 MW; B7034936A10BFFF0 CRC64;
MLSSTDFTSA SWELAVCVDH PNEEQQKDVT LRVSGDLHVG GVMLKLVEQI NISQDWSDFA
LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA
VSDICKTLNI RRSEELSLLK PPGDYFKKKK KKDKNNKEPI IEDVLNLESS PTASGSSVSP
GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSPEA LADMYQPRSL
VDKAKLNAGW LDSSRSLMEQ GIQEDEQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI
LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFTSESEV DEIEAALSNL EVTLEGGKAD
SLLEDITDIP KLADNLKLFR PKKLLLKAFK QYWFVFKDTS IAYFKNKELE QGEPVEKLNL
RGCEVVPDVN VAGRKFGIKL LIPVADGMNE MYLRCDHENQ YAQWMAACML ASKGKTMADS
SYQPEVLNIL SFLRMKNRNS ASQVASSLKN MDMNPECFVS PRCAKKHKSK QLAARILEAH
QNVAQMPLVE AKLRFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVSYNRL IKIDAATGIP
VTTWRFTNIK QWNVNWETRQ VVIEFDQNVF TAFTCLSADC KIVHEYIGGY IFLSTRSKDQ
NETLDEDLFH KLTGGQD
//