ID A0A452H8N5_9SAUR Unreviewed; 677 AA.
AC A0A452H8N5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000010927.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000010927.1}
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 AlphaFoldDB; A0A452H8N5; -.
DR STRING; 38772.ENSGAGP00000010927; -.
DR Ensembl; ENSGAGT00000012521.1; ENSGAGP00000010927.1; ENSGAGG00000008489.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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; 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; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 377..473
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
SQ SEQUENCE 677 AA; 77613 MW; 2648D0024DB1E461 CRC64;
MTSSKEYGSN SWELIVTVDH QYEEEQKEFT LRVAGDLHIG GVMLKLVEQI NLSRDWSDYA
LWWEQKNCWL LKTHWMLDKC GVQADAKLLF TTQHKMLRLC LPNMKTVRLK VSFSSVVFKA
VSDICKTLNI RRSEELSLLK QSEDTLKKKK KKDKNNKEPV IEDILNLYNS PVISGSPASP
GLFSKTMTPI YDPVNGTPVP STMTWFSDSP LTAPNCSILA FSHPNCSPET LAEMYQPRTL
ADRAKLNAGW LDSSRSLMEQ SVQEDDQLLL RFKYYTFFDL NPKYDAVRIN QLYEQARWAI
LLEEIDCTEE EMLIFAALQY HLSKLSLSSE AQDFTHESEV DEVEAALSNL EVTLEGGKMD
NILEDITDIP KLADNLRLFR PKKLTLKAFK QYWFVFKDTS VSYFKNKEAG HGEPIEKLNL
KGCEVVPDVN VAGRKFGIKL LIPVADGMNE VYLRCDNENQ YACWMAACVL AAKGRTMADS
SYQPEVHKIL SFLKMKNRTT SPQAVSDPES MDMKPERFVS PRYAKKYKSK QLAARILEAH
QNVAQMPLVE AKLRFIQAWQ SLPEFGLTYY IVRFKGSKKD DLLGISYNRL IRIDAATGDP
ITTWRFSSMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY IFLSTRSKDQ
NETLDEDLFH KLTGGRE
//
