ID A0A452GNA8_9SAUR Unreviewed; 917 AA.
AC A0A452GNA8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
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:ENSGAGP00000003210.1, 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:ENSGAGP00000003210.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452GNA8; -.
DR Ensembl; ENSGAGT00000003701.1; ENSGAGP00000003210.1; ENSGAGG00000002535.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13184; FERM_C_4_1_family; 1.
DR CDD; cd17203; FERM_F1_EPB41L3; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR030691; Band4.1-L3_FERM_F1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR007477; SAB_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR PANTHER; PTHR23280:SF20; BAND 4.1-LIKE PROTEIN 3; 1.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF04382; SAB; 1.
DR PIRSF; PIRSF002304; Membrane_skeletal_4_1; 2.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 114..395
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 103210 MW; A9F09C011F7F5F1F CRC64;
MTTQSGSDSE SKDQDQDQQE APAQQGTAGA QPQDHQQQQL SEEHQNAIDQ FSAVAAHSTP
VKKEQVTDRE REFAAAAAKQ LEYQQFEDDK LSQKSSSSKL SRSPLKIVKK PKNMQCKVML
LDGSEYGCEV EKRSRGQILF DKVCEHLNLL EKDYFGLTYR DMENQKNWLD PAKEIKKQMR
SGAWQFSFNV KFYPPDPSQL SEDITRYYLC LQLRDDIVSG RLPCSFVTLA LLGSYTVQSE
LGDYDPDEYG SDYVSEFRFA PNHTKELEDK VIELHKSHRG MTPAEAEMHF LENAKKLSMY
GVDLHHAKDS EGVEIMLGVC ASGLLIYRDR LRINRFAWPK VLKISYKRNN FYIKIRPGEF
EQFESTIGFK LPNHRAAKRL WKVCVEHHTF FRLLLPEAPP KKFLTLGSKF RYSGRTQAQT
RRASALIDRP APYFERSSSK RYTMSRSLDG EVGTGQYATT KGISQTNLIT TVTPEKKAEE
ERDEEEGKKK GEEITPVSAI RHDTKTDSEQ TDTAADGETT ATESDQEEDG DLKAQNSLIK
RIKGENVYVK HSNLMLEELD KNQEDLMKHQ TNISELKRTF LETSTDTTVS NEWEKRLSTS
PVRLAARQEE APMIEPLVPE ETKEEREKSE KLIFLQKGST TFMESQKTET KTSQEISVSE
MKEEVQPYQD SVKKVVQETV VVEERYVTNV HASGDAVKLA GDQLDAMAQA VSAVASSMKG
KEGSAVTEGT KEEKREEADK AVTKREGIAA ASHQQEEEQS ATVHISDTLE RKPHFEQSPV
VKTETISFGS VSPGGEKLEM STKEVPIVHT ETKTITYESS QADSGADSEP GVLMSAQTIT
SETTSTTTTT HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT
KVVVHKETEI TPEDGED
//
