RELCH_DANRE
ID RELCH_DANRE Reviewed; 1189 AA.
AC Q6P6Y1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=RAB11-binding protein RELCH homolog;
DE AltName: Full=LisH domain and HEAT repeat-containing protein KIAA1468;
DE AltName: Full=RAB11-binding and LisH domain, coiled-coil and HEAT repeat-containing protein RELCH;
GN Name=relch; ORFNames=zgc:66014;
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 MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May regulate intracellular cholesterol transport.
CC {ECO:0000250|UniProtKB:Q9P260}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome
CC {ECO:0000250|UniProtKB:Q9P260}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9P260}.
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DR EMBL; BC061956; AAH61956.1; -; mRNA.
DR RefSeq; NP_957138.1; NM_200844.1.
DR AlphaFoldDB; Q6P6Y1; -.
DR STRING; 7955.ENSDARP00000055445; -.
DR PaxDb; Q6P6Y1; -.
DR GeneID; 393817; -.
DR KEGG; dre:393817; -.
DR CTD; 57614; -.
DR ZFIN; ZDB-GENE-040426-1507; relch.
DR eggNOG; KOG0211; Eukaryota.
DR InParanoid; Q6P6Y1; -.
DR OrthoDB; 73423at2759; -.
DR PhylomeDB; Q6P6Y1; -.
DR PRO; PR:Q6P6Y1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR040362; RELCH.
DR PANTHER; PTHR32059; PTHR32059; 1.
DR Pfam; PF02985; HEAT; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
DR PROSITE; PS50896; LISH; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endosome; Golgi apparatus; Lipid transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..1189
FT /note="RAB11-binding protein RELCH homolog"
FT /id="PRO_0000313095"
FT DOMAIN 229..261
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 574..612
FT /note="HEAT 1"
FT /evidence="ECO:0000305"
FT REPEAT 613..652
FT /note="HEAT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REPEAT 977..1015
FT /note="HEAT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..205
FT /evidence="ECO:0000255"
FT COILED 326..373
FT /evidence="ECO:0000255"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 132131 MW; 128129EAE270FDD7 CRC64;
MAAGNVNPFN VSDSEEEAEQ RQDGADTERS PSDEAQGHSL GPFSPPAYSD PAALLSSNRT
SPSVDGIPAS AAAVSGIGAE TRVSLDAIAA QLLRDQYILT ALELHTELLE AGRELPRLRD
YFSNPGNFER QSGTPPACKE QGVGPGGPLN RAGSISTLDS LDFARYSDDG NRESDERVAV
LEFELRKAKE TIQALRANLT QAAECEIASQ ERKNYKSSPE TQEPIRPLEK RALNFLVNEY
LLKNEYKLTS ITFSDENDDQ DFELWDDVGL NIPKPPDLLQ LYRNCGNSQP LHRDTVDVAV
SVDPSDLPAD YFTQEPVQQT DVIQQQQQQE VVQELEYQIS LLNSEKQSLA EQIKKLQSDI
QALQRNVSSE LTAGVKSIQS KENPKCDKPP LDNGQYLDIR GVTETDSSSD TTKTSTSTTI
ATDCTENSTT ATQPHSKLKA NGQQSKSSVQ FDQPNRKLSP AFHQALLSFC RMSADSRLGS
EVSRIADSEQ SVMLMLGRCL PHIVPNVLLA KREELIPLIL CTACLHPEPK ERDQLLHILF
NLIKRPDDEQ RQMILTGCVA FAQHVGPTRV EAELLPQCWE QINHKYPERR LLVAEACGAL
APYLPKEIRS SLVLSMLQQM LADDKADMVR EAVVKSLGVI MGYIDDPDKY SQGFELMLLS
LGDPSERVVS ATHQVFIPAF AAWCTELGNL QSQLIPSLLT RIEKLLKQGE YGLDEHKLHM
YLSALQSLIP SLFAVLLQNA PFTSRVKLQG DVPPIEVTRF PRPASPLQDV ATIVGSREQL
AVLLHLYDHQ LQHEGTTGWD SLLWVVNQFL PQIIDIVGRI NVTSSTCVHE FSRFFWRLCR
TFGKIFTNTK VKPQFQEILR LSEENVDATA GNGILTKATV PIYATGVLTC YNQEEDRKLL
VGFLEDVMTT LSLSHAPLDS LKASFVELGA NPAYHELLLT VLWYGVVHTS ALVRCTAARM
FELLVKGVNE TLVAQRVVPA LITLSSDPEI SVRISTIPAF GTIMETVTQK ELLERVKMQL
ASFLEDPQYQ DQHSLHMEII KTFGRVGPNA EPRFRDEFVL PHLHKLALCN NQQTVESKRI
DIATQLFEAY SALSCCFISE ELMVNHFLPG LRCLRTDMEQ LSPEHEVILS SMIKECEIKV
ENKGIGEAQG SISIAASLVG EDAKTKFLSK MGQLTTSGAM LANVFQRKK