FA83H_DANRE
ID FA83H_DANRE Reviewed; 1192 AA.
AC Q1LVV0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein FAM83H {ECO:0000305};
GN Name=fam83h {ECO:0000250|UniProtKB:Q6ZRV2}; ORFNames=si:ch211-199g17.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: May play a role in keratin cytoskeleton disassembly.
CC {ECO:0000250|UniProtKB:Q6ZRV2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q6ZRV2}. Note=Colocalizes with keratin
CC filaments. {ECO:0000250|UniProtKB:Q6ZRV2}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
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DR EMBL; BX649384; CAK04374.1; -; Genomic_DNA.
DR RefSeq; NP_001038555.1; NM_001045090.2.
DR AlphaFoldDB; Q1LVV0; -.
DR SMR; Q1LVV0; -.
DR STRING; 7955.ENSDARP00000080573; -.
DR PaxDb; Q1LVV0; -.
DR PRIDE; Q1LVV0; -.
DR Ensembl; ENSDART00000086138; ENSDARP00000080573; ENSDARG00000060830.
DR GeneID; 565918; -.
DR CTD; 565918; -.
DR ZFIN; ZDB-GENE-030131-6729; fam83hb.
DR eggNOG; ENOG502QW7K; Eukaryota.
DR GeneTree; ENSGT00940000159342; -.
DR InParanoid; Q1LVV0; -.
DR OrthoDB; 84242at2759; -.
DR PhylomeDB; Q1LVV0; -.
DR PRO; PR:Q1LVV0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000060830; Expressed in zone of skin and 19 other tissues.
DR ExpressionAtlas; Q1LVV0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:1990254; F:keratin filament binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0044380; P:protein localization to cytoskeleton; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09188; PLDc_FAM83H_N; 1.
DR InterPro; IPR012461; FAM83_N.
DR InterPro; IPR041996; PLDc_FAM83H_N.
DR Pfam; PF07894; FAM83; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1192
FT /note="Protein FAM83H"
FT /id="PRO_0000324490"
FT REGION 435..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 134941 MW; 412F6D3BAD00BEFB CRC64;
MARRSQSSSL GDNPLDPNYL RPHYREEYRM AIDALVEDDI EGYYNFLQNA NVVDFLSRSE
IENIKSTVQT PQSAGNVPEL PYGEIDQDES SDTYWPLHSD LDAPGLDLGW PMQQHSFVGP
TEVTMLVNPA EPERPSIKEQ ARRLIKNAHQ VIAVVMDIFT DVDIFSDLLE AAARHVPVYI
LLDEQNAHYF VNMVASCKVN LEMIHMMRVR TVSGVTYFCR TGKSFKGQVM DRFLLTDCRA
VISGNYSFMW SFEKIHRCIA HLFLGELVAT FDEEFRILFA QSQPLVVENA LVPMPQDSYL
GNQFGLKRTQ SLRNPRGYLR QPELGGYQYG DRLDSILPFR RDDPFRHTIE PSAGPMQVTK
YATQQFRMQQ SFLDQGRSML ASRQLEMNAF KRHSYAEGTR ETYASSRQYM KQRVMNNLEE
TESHYQREQH YYQSEGMGHD DRGHYDRFNY GLADQHSDSG YPPELEAPGN INVLSSDDLK
SDSEKQYNIG GRYDPQGHKR PAAGHAYACQ SSPTQPHPPD QKQLFSTGDQ VRQSQDPSVK
QGLRSWRINS YLSTYEDGGE EGLHQPMGSD AFEDSHQQPD SRLYGSEGPG IHSNIRERPN
IPTKPNLDLR PRFGKPIIQD RNQVKDNTSD LGPTSTDTLK PAISASSLAS STDNEKELAE
PREISITKHE SFRTRINPML QRSSRLRSSL IFSSSKLEQH NSSQAKSGGE LQEEKEESEP
IRYSSIVAEI LEKRRSLSRE PFDWNKHKKA DEKDVKHAST GDLTTIQDTK EEPIKEKEKP
DNPKPEENKV TQPTVPSASQ QITSSLNMND PASRLQYFKD QQEKRKTSKL ELDLGTKSQE
AAIKKPETLD TATKVPDVLL TSEQSTVKAQ EPTVSQTDPV PHRPVIETKP KPSEVSVDRP
YTTNKTLTES IADAPKKEPV KEPTKSLKPF PSPKFLKPFK SSQSSSRRIS CGEEILTDAT
DAEKSELKKS RSFSTSGMSR TESRESLSSL GNSESKDTKA LDFLKKQTQR LKGILGPKGD
KKHSGVSNSQ EDKSMKTVPE VQEEISDKGK PSESISSSTA VENKPSAKPT TSRYQSSTSN
IIFSSNLRDD TKVILEQISA NSQKTRQQNE ESGKGDGGKD DVANSPFQSR NRFSRAPVNP
QERDNLLKRI ESMRKEKKVY SRFEVLYRSR EECCWERGSV EQANQFLIKS IE
