FHI1B_RAT
ID FHI1B_RAT Reviewed; 791 AA.
AC Q66H54;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543; SER-547; THR-708 AND
RP SER-716, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC082011; AAH82011.1; -; mRNA.
DR RefSeq; NP_001005538.2; NM_001005538.2.
DR RefSeq; XP_006229994.1; XM_006229932.3.
DR AlphaFoldDB; Q66H54; -.
DR STRING; 10116.ENSRNOP00000023502; -.
DR iPTMnet; Q66H54; -.
DR PhosphoSitePlus; Q66H54; -.
DR PaxDb; Q66H54; -.
DR GeneID; 293343; -.
DR KEGG; rno:293343; -.
DR UCSC; RGD:1359585; rat.
DR CTD; 84067; -.
DR RGD; 1359585; Fam160a2.
DR VEuPathDB; HostDB:ENSRNOG00000017408; -.
DR eggNOG; KOG3695; Eukaryota.
DR HOGENOM; CLU_007807_1_0_1; -.
DR InParanoid; Q66H54; -.
DR OMA; CLDWDSG; -.
DR OrthoDB; 141539at2759; -.
DR PRO; PR:Q66H54; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017408; Expressed in testis and 19 other tissues.
DR Genevisible; Q66H54; RN.
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; 2.
DR Pfam; PF19314; DUF5917; 1.
DR Pfam; PF19311; KELAA; 1.
DR Pfam; PF10257; RAI16-like; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..791
FT /note="FHF complex subunit HOOK interacting protein 1B"
FT /id="PRO_0000253862"
FT REGION 465..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2I3"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2I3"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT MOD_RES 708
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 791 AA; 86272 MW; 9986D733C9B25394 CRC64;
MEKMNWLSRL ASRVPGHRVP QGASLQTPVM ADPETCLMVF KNHWSQVVRI LERQGSRAAA
GGADDLSAVR NHTYQMLTLL AEDRAVPSAP SGPGPLLEFA LREDLLSRVL TWQLQWDEFG
DGVEERRAEQ LKLFEMLVSE ARQPLLRHGP VREALLALLD ACGRPVPSSP ALDEGLVLLL
SQLCVCVARE PSLLEFFLQP PPEPGAAPRL LLFSRLVPFV HREGTLGQQA RDALLLLMAL
SDGSPTVGRY IADHSYFCPV LATGLSALYS SLPRKIEVPG DDWHCLRRED WIGVPALALF
MSSLEFCNAV IQVAHPLVQK QLVDYIHNGF LVPVMGPALH KTSVEEMIAS TAYLELFLRS
ISEPALLRTF LRFLLLHRHD THTILDTLVA RIGSNSRLCM VSLSLFRTLL NLSCEDVLLQ
LVLRYLVPCN HVMLSQKPAV RDVDLYGRAA DKFLSLIPRC CRHHAPSPPR PEHASWARGG
PSREPGRRED ITGPGSPSVD SSSVVTVPRP STPSRLALFL RQQSLGGSES PGPAPRSPGL
TASPTSSPGR RPSPAEEPGP FMAVLFAKLE NMLQNSVYVN FLLTGLVAQL ACHPQPLLRS
FLLNTNMVFQ PSVKSLLQVL GSVKNKIESF AASQEDFPAL LSKAKKYLIA RGKLDWAEGP
TAGPTPRRSD SLVRSRRPSL GELLLRHAHS PTRARQAVQV LQPGRDGTGL GLGGGSPGAS
TPVLLPRGGA SERQGEALRV KNAVYCAVIF PEFLKELAAI SQAHAVTSPF LLDTSEEVSV
PPISGFGPLN P
