ID   RELCH_XENTR             Reviewed;        1196 AA.
AC   Q08BT5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=RAB11-binding protein RELCH homolog;
DE   AltName: Full=LisH domain and HEAT repeat-containing protein KIAA1468;
DE   AltName: Full=RAB11-binding protein containing LisH, coiled-coil, and HEAT repeats;
GN   Name=relch; Synonyms=kiaa1468;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) 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; BC124571; AAI24572.1; -; mRNA.
DR   RefSeq; NP_001120526.1; NM_001127054.1.
DR   AlphaFoldDB; Q08BT5; -.
DR   STRING; 8364.ENSXETP00000052078; -.
DR   PaxDb; Q08BT5; -.
DR   GeneID; 100145663; -.
DR   KEGG; xtr:100145663; -.
DR   CTD; 57614; -.
DR   Xenbase; XB-GENE-985071; relch.
DR   eggNOG; KOG0211; Eukaryota.
DR   InParanoid; Q08BT5; -.
DR   OrthoDB; 73423at2759; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   ExpressionAtlas; Q08BT5; differential.
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; IPR021133; HEAT_type_2.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR040362; RELCH.
DR   PANTHER; PTHR32059; PTHR32059; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
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..1196
FT                   /note="RAB11-binding protein RELCH homolog"
FT                   /id="PRO_0000313096"
FT   DOMAIN          234..266
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REPEAT          620..659
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          984..1022
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          333..374
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        27..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..70
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1196 AA;  132512 MW;  548ADD2498008B36 CRC64;
     MAAPAAGSGP GGSSGGITGG AGGSLGVVGP STSTSSVNPF LSDSEEEEDG GEEEEEEEED
     DNEEDDEDVS PLNERPAASL ASRYLQDEAD STLLPSAGPR LCLQPGEPGR VPLDAVAAQL
     LRDQLLLTAL ELHTELLESG RELPRLRDYF SNPGNFERAT AAPPGFGGNT TASTGGQLNR
     AGSISTLDSL DFARYSDDGN RETDERVAEN EVPLQERKNY KSSPEIQEPI KPLEKRALNF
     LVNEYLLKNN NKLTSITFSD ENDDQDFELW DDVGLNTPKP PDLLQLYRNL SNHQTVSKDV
     ADIAVGVIEG DLEPIQAVKQ IAPDSHISQQ AAIIKELEDK IILCNNEKAA LLEQIGNLER
     QIESLQKENS ASGVCSAAPP TSDRLQSQTS EESDHYIDIQ ITDSDAKCEG TEERLPFQQS
     ECEPVCQVSE DIPPSPELAK IRKTTLLSAP PSKAGVHFDK PNRKLSPAFH QALLSFCRMS
     ADSRLGSEVS QIADSENGVM KMLGRCLPHI VPNVLLAKRE ELIPLILCTA CLHPESKERD
     QLLHILFNLI KRPDDEQRQM ILTGCVAFAR HVGPTRVEAE LLPQCWEQIN HKYPERRLLV
     AESCGDLAPY LPKEIRSSLV LAMLQQMLME DKADMVREAV IKSLGIIMGY IDDPDKYSQG
     FELLLTALGD PSERVVSATH QVFLPAYAAW TMELGNLQSH LIPTLLSKIE KLLKEGEHGL
     DEHKLHMYLS ALQSLIPSLF ATVLQNAPFT SKAKLQGEVP QIEVTRFPRP VSPLQDVATI
     IGSREQLAVL LQLYDYQLEH EGTTGWESLL WVVNQLLPQL IEIVGRITVT STASVHEFSR
     FFWRLCRTFG KIFTNTKVKP QFQEILRLSE ENIDSTAGNG VLTKATVPIY ATGVLTCYNQ
     EEDRKLLVGF LEDVMTMLSL SHAPLDSLKA SFVELGTNPA YHELLLTVLW YGVVHTSALV
     RCTAARMFEL LVKGVNETLV AQRVVPALIT LSSDPEISVR IATVPAFGTI METVTQRELL
     ERVKMQLASF LEDPQYQDQH SLQTEIIRTF GRVGPNAEPR FRDDFVLPHL HKLSFVNNQQ
     SVDSKRLDIA THLFEAYSAL SCCFISEELM MNHFLPGLRC LRTDMEQLSP EHEVILSSMI
     KECEQKVENK TVQEPQGSMS IAASLVSEDT KTKFLNKMGQ LTTSGAMLAN VFQRKK