ID A0A452GMV3_9SAUR Unreviewed; 1234 AA.
AC A0A452GMV3;
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:ENSGAGP00000003170.1, 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:ENSGAGP00000003170.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452GMV3; -.
DR Ensembl; ENSGAGT00000003650.1; ENSGAGP00000003170.1; 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 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 815..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1079
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 954..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 138535 MW; 5AEE4AE5A4ADBFE2 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 TFMESQPREI EKKLQEGESA
GTVVTSHQII FQKSVPSSLE GTEDWVIVDK IPTEVVDGES KKIVTYKVMT VRSKTGDIPP
EILKSSTIEM QSFEDLENEI QSKEENKQKM YTLGKSYDTI SGKIVTMTSK AKEGEKTVQS
SLEAFQKMER GMPESVKIIP VVAEYEILEP ITDEKARRGS DVQSTKRKLS ESLTPIKEAE
SQLHSPEEES LKKAQKMDQD FHGTLGGLQF GRAEKHLDSE ALKAGAFGRK DKSLSEWRYS
REQPFTIATA HYVSESSASR VVTKQSSSEK TLDGSDIFSL LESARKPTEF IGEVTSTSHS
RAQKTETKTS QEISVSEMKE EVQPYQDSVK KVVQETVVVE ERYVTNVHAS GDAVKLAGDQ
LDAMAQAVSA VASSMKGKEG SAVTEGTKEE KREEADKAVT KREGIAAASH QQEEEQSATV
HISDTLERKP HFEQSPVVKT ETISFGSVSP GGEKLEMSTK EVPIVHTETK TITYESSQAD
SGADSEPGVL MSAQTITSET TSTTTTTHIT KTVKGGISET RIEKRIVITG DADIDHDQAL
AQAIKEAKEQ HPDMSVTKVV VHKETEITPE DGED
//
