ID A0A452ERP0_CAPHI Unreviewed; 1033 AA.
AC A0A452ERP0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=FERM domain containing 4B {ECO:0000313|Ensembl:ENSCHIP00000014518.1};
GN Name=FRMD4B {ECO:0000313|Ensembl:ENSCHIP00000014518.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000014518.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000014518.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000014518.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452ERP0; -.
DR Ensembl; ENSCHIT00000022316.1; ENSCHIP00000014518.1; ENSCHIG00000015488.1.
DR GeneTree; ENSGT01020000230354; -.
DR OMA; RAPHNPY; -.
DR Proteomes; UP000291000; Chromosome 22.
DR Bgee; ENSCHIG00000015488; Expressed in uterine horn and 16 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13191; FERM_C_FRMD4A_FRMD4B; 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; IPR019749; Band_41_domain.
DR InterPro; IPR021774; CUPID.
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; IPR047176; FRMD4A/B.
DR InterPro; IPR041785; FRMD4A/B_FERM_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46079; FERM DOMAIN-CONTAINING PROTEIN 4; 1.
DR PANTHER; PTHR46079:SF1; FERM DOMAIN-CONTAINING PROTEIN 4B; 1.
DR Pfam; PF11819; CUPID; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR SMART; SM00295; B41; 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; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 59..359
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 634..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1033 AA; 117592 MW; 7E429B2AF7562C66 CRC64;
MASVFMCGVE DLLFSGSRFV WNLTVSTLRR WYTERLRACH QVLRTWCGLR EVYQMTEGRH
CQVCLLDDRR LELLVQPKLL SRELLDLVAS HFNLKEKEYF GITFTDDTGQ QNWLQLDHRV
LDHDLPKKPG PTILCFSVRF YIESISFLKD KTTVELFFLN AKSCVHKGQI EVDSETIFRL
AALILQVRTD KPDENARKDL KTLPAFPTKT LQEHPSLAYC EDRVIEHYLK IKGLTRGQAV
VQYMKIVEAL PTYGVHYYAV KDKQGLPWWL GISYKGIGQY DLQDKVKPRK LFQWKQLENL
YFREKKFAVE VHDPRRISVS RRTFGQSGLF VQTWYANSSL IKSIWVMAIS QHQFYLDRKQ
SKAKIPSARS LDDIAMDLTE TGAPRVSKLV TLEAKSQFIM ASNGSLISSG SQDSEVSEEQ
KREKILELKK KEKLLQEKLL KKVEELKKIC LREAELTGKM PKEYPLNVGE KPPQVRRRIG
TAFKLDDNLL PSEEDPALQE LESNFLIQQK LVEAVKKLAS EPDLCKTVKK KRKQDYTDAV
KKLQEIENAI NEYRIRCGKK PSQKATVILP EDIIPSESSS LSDTTTCDDP NDTFTLAGQR
SSSVPHSPRI LPPKSLGIER IHFRKSSINE QFVDTRQSRE MLSTHSSPYK TLERRPQGGR
SMPTTPVLTR NAYSSSHLEP EPSSQHCRQR SGSLESQSHL LSEMDHEKPF FSLSKSQRSS
STEILDDGSS YTSQSSTEYY CTTPVAGPYY TTQTLDTRSR GRRRSKKQNV STSNSGSMPN
LAHKDSLRNG VYPKSQEQPS SSCYIAGYTP YAECDLYYAG GYVYENDTEG QYSVNPSYRS
STHYGYDRPR DCSRSFHEDE VDRVPHNPYA TLRLPRKGAA KSEHITKNIH KALVAEHLRG
WYQRASGQKE QGHSAQTSFD SDRGSQRSLG FAGLQVPCSP SSRASSYSSV SSTNASGNWR
TQITLGLSEY EIPAHSSYTS CYSNIYNPLP SPGRPYTETS QLDGTEGSRL EDSLGSSEQR
LFWHEDSKPG TLV
//
