FHI1B_DANRE
ID FHI1B_DANRE Reviewed; 1124 AA.
AC B0V207;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=FHF complex subunit HOOK interacting protein 1B;
DE Short=FHIP1B;
DE AltName: Full=FTS and Hook-interacting protein homolog;
DE Short=FHIP;
GN Name=fhip1b; Synonyms=fam160a2; ORFNames=si:ch211-39h10.1;
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: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF
CC complex may function to promote vesicle trafficking and/or fusion via
CC the homotypic vesicular protein sorting complex (the HOPS complex). FHF
CC complex promotes the distribution of AP-4 complex to the perinuclear
CC area of the cell. {ECO:0000250|UniProtKB:Q8N612}.
CC -!- SUBUNIT: Component of the FTS/Hook/FHIP complex (FHF complex), composed
CC of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of
CC proteins HOOK1, HOOK2, and HOOK3. The FHF complex associates with the
CC homotypic vesicular sorting complex (the HOPS complex).
CC {ECO:0000250|UniProtKB:Q8N612}.
CC -!- SIMILARITY: Belongs to the FHIP family. {ECO:0000305}.
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DR EMBL; CR936366; CAQ15357.1; -; Genomic_DNA.
DR RefSeq; NP_001124329.1; NM_001130857.1.
DR RefSeq; XP_005167711.1; XM_005167654.3.
DR AlphaFoldDB; B0V207; -.
DR STRING; 7955.ENSDARP00000101150; -.
DR PaxDb; B0V207; -.
DR PeptideAtlas; B0V207; -.
DR PRIDE; B0V207; -.
DR Ensembl; ENSDART00000110582; ENSDARP00000101150; ENSDARG00000078188.
DR GeneID; 100001896; -.
DR KEGG; dre:100001896; -.
DR CTD; 84067; -.
DR ZFIN; ZDB-GENE-070912-291; fhip1b.
DR eggNOG; KOG3695; Eukaryota.
DR GeneTree; ENSGT00950000182936; -.
DR HOGENOM; CLU_007807_0_0_1; -.
DR InParanoid; B0V207; -.
DR OMA; CLDWDSG; -.
DR OrthoDB; 141539at2759; -.
DR PhylomeDB; B0V207; -.
DR TreeFam; TF313941; -.
DR PRO; PR:B0V207; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000078188; Expressed in retina and 20 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR019384; FHIP.
DR InterPro; IPR045669; FHIP_C.
DR InterPro; IPR045668; FHIP_KELAA_motif.
DR PANTHER; PTHR21705; PTHR21705; 1.
DR Pfam; PF19314; DUF5917; 1.
DR Pfam; PF19311; KELAA; 1.
DR Pfam; PF10257; RAI16-like; 1.
PE 3: Inferred from homology;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1124
FT /note="FHF complex subunit HOOK interacting protein 1B"
FT /id="PRO_0000379001"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 123015 MW; 7794E8C4F55AD319 CRC64;
MSWLSRLNPR GPGTRTGRHA APSSPCTADP ETCLMVFENH WRQVSGVLKQ RESSVGGFAD
DLTAVRNHTD QMLCLLAEER PAGGDIDSPA MGPILEMVVA ENILEELVQW HVCRGLDPDS
QLELLKLFEM LIGQSHQPLL LHSAVLQPLL SLLGACVDPQ MGCPPALESS LVLLLNQVCV
SMAKETAVLE LLFRCGSVQQ GPTNLLIFSL LVPFIHRDGA LGQQARDALL LVMATSASNH
AVARHITENS YFCPVLATGL SGLYSSLPRK IEVRGDDWHA LRREDWIGVS SLVLFMNSLE
FCNAVVQVAH PLVRCQLLDY LHNGFLVPVM GPALHKSSVD EMIASTAYLD LFLRCITETS
LLKTFLRFIL LHHHDNDTIL DTLLTRISSN SRLCMVSLSL FKTLLSLNCE DLMLQLVLRY
LLPCTHVMLS QRRAVRETDL YGKSADKFLS LIPECCRITS APSGERDEEP AFWGKVLGSP
TSESPVHPRP STPSRLALFI RQQSSGGQAN PSSSGSENAP SSPRGSVSSP LSPDSPMHQL
SDFSEGETGY LEYLRDARKG IELCSWGCRD WSAPYDGENP SPNSAPLPPP PPTSNPSLSM
VQEHFSVMDP TQQRAAVVAA ARAEWSSSDR DSGEWDVTIS KNCISLTPRS KKRSLLPSSI
PLQSSSSASV STEITGASET VYQHSRSTPH PALYNGMGQV EFTDSVDERM EAKKVKRDSD
VNSGMVETGM NGSMGPVDYN DFHVGSTLKS SQVQLKPHLQ HHTSVPSSTQ ECLPTESHRL
SPVLGLTESS AASRGSESVE RLIEELLERA PSEPLSGDSK CQGISIEAFH QELRELEERV
RERRVSSRSS EESSRESRTA PLPSLTDEDC LPVETEQRSS ETKPDSSTTG VFSPARPLGQ
PLAQPYTGPF ITVLFSKLEN MMQNSLYVNI LLTGVVFQLA CYPQPLLRSF LLNANMVFQP
SVKSLIQVLG TVKNRIEVFA AAHEDFPAML RKARRFLVAR GKLDWSDSAM GVPSLRRSDS
LIKSRKPSLG DLILRHTNSP TRARHAAQLA LAHVRDGGQS LHSALFRGSA ASGASGLEKQ
AEALRVKNAV YCAVIFSEFL KELAALAQEH AVALPFPPSQ GTEE
