FHI1B_PONAB
ID FHI1B_PONAB Reviewed; 972 AA.
AC Q5R8V2; Q5REW8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=FHF complex subunit HOOK interacting protein 1B;
DE Short=FHIP1B;
DE AltName: Full=FTS and Hook-interacting protein;
DE Short=FHIP;
GN Name=FHIP1B; Synonyms=FAM160A2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH89689.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR857397; CAH89689.1; ALT_FRAME; mRNA.
DR EMBL; CR859647; CAH91808.1; -; mRNA.
DR RefSeq; NP_001126049.1; NM_001132577.1.
DR RefSeq; NP_001128746.1; NM_001135274.1.
DR AlphaFoldDB; Q5R8V2; -.
DR STRING; 9601.ENSPPYP00000004071; -.
DR GeneID; 100172999; -.
DR GeneID; 100189640; -.
DR KEGG; pon:100172999; -.
DR CTD; 84067; -.
DR eggNOG; KOG3695; Eukaryota.
DR InParanoid; Q5R8V2; -.
DR Proteomes; UP000001595; Unplaced.
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 2: Evidence at transcript level;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..972
FT /note="FHF complex subunit HOOK interacting protein 1B"
FT /id="PRO_0000253861"
FT REGION 465..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2I3"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2I3"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H54"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H54"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT CONFLICT 477..478
FT /note="AR -> VN (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="S -> G (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="Q -> L (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="H -> R (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="R -> K (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="V -> A (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="N -> S (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="P -> L (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="R -> H (in Ref. 1; CAH89689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 972 AA; 105466 MW; E99395EA83C4ADB0 CRC64;
MERMNWLSRL ASRGPGHRIP QGANLQTPVM ADPETCLMVF KNHWSQVVRI LERQGPRAAP
GGADDLSAVR NHTYQMLTLL AEDRAVPSAP TGPGPLLEFA PHEDLLTRVL TWQLQWGELG
DGVEERRAEQ LKLFEMLVSE ARQPLLQHGP VREALLTLLD ACGRPVPSSP ALDEGLVLLL
SQLCVCVAQE PSLLEFFLQP PPEPGAAPRL LLFSRLVPFV HREGTLGQQA RDALPLLMAL
SAGSPTVGRY IADHSYFCPV LATGLSALYS SLPRRIEVPG DDWHCLRRED WLGVPALALF
MSSLEFCNAV IQVAHPLVQK QLVDYIHNGF LVPVMGPALH KTSVEEMIAS TAYLELFLRS
ISEPALLRTF LRFLLLHRHD THTILDTLVA RIGSNSRLCM VSLSLFRTLL NLSCEDVLLQ
LVLRYLVPCN HVMLSQKPAV RDVDLYGRAA DKFLSLIPRC CRHHAPSPPR PEHASWARGP
GSPSVDSSSV MTVPRPSTPS RLALFLRQQS LSGSESPGPA PCSPGLSASP ASSPGRRPTP
AEEAGELEDN YLEYQREARR GVDHCVRACR TWSAPYDGER PSPEPSPFGS RTKKRSLLPE
EDRNNVGEGE EEELGSRGLA GGAGEGPGHL PPPQLNGVPG SWPEGAKRVR LVPKEGVGEL
LEGISEGMAG LEGFGQELRE LEVALSNGGT GSESPLEPPL PLEEEEAYES FTCPPEPPGP
FLNSPLRTPN QLPSQPFTGP FMAVLFAKLE NMLQNSVYVN FLLTGLVAQL ACHPQPLLRS
FLLNTNMVFQ PSVKSLLQVL GSVKNKIENF AASQEDFPAL LSKAKKYLIA RGKLDWAEGP
AAGPAPRRSD PLVKSRRPSL GELLLRHARS PTRARQAAQL VLQPGRDGAG LGLSGGSPGA
STPVLPTRGG APERQGEALR VKNAVYCAVI FPEFLKELAA ISQAHAVTSP FLLETSEEGS
GPLISGCGPL NP
