RELCH_HUMAN
ID RELCH_HUMAN Reviewed; 1216 AA.
AC Q9P260;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=RAB11-binding protein RELCH {ECO:0000305};
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 {ECO:0000312|HGNC:HGNC:29289};
DE AltName: Full=RAB11-binding protein containing LisH, coiled-coil, and HEAT repeats {ECO:0000303|PubMed:29514919};
GN Name=RELCH {ECO:0000303|PubMed:29514919, ECO:0000312|HGNC:HGNC:29289};
GN Synonyms=KIAA1468 {ECO:0000303|PubMed:10819331};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 266-1216 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-182; THR-183 AND
RP SER-186, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-20; SER-22 AND SER-180, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-453, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-929.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=29514919; DOI=10.1083/jcb.201709123;
RA Sobajima T., Yoshimura S.I., Maeda T., Miyata H., Miyoshi E., Harada A.;
RT "The Rab11-binding protein RELCH/KIAA1468 controls intracellular
RT cholesterol distribution.";
RL J. Cell Biol. 217:1777-1796(2018).
CC -!- FUNCTION: Regulates intracellular cholesterol distribution from
CC recycling endosomes to the trans-Golgi network through interactions
CC with RAB11 and OSBP (PubMed:29514919). Functions in membrane tethering
CC and promotes OSBP-mediated cholesterol transfer between RAB11-bound
CC recycling endosomes and OSBP-bound Golgi-like membranes
CC (PubMed:29514919). {ECO:0000269|PubMed:29514919}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:29514919}.
CC Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29514919}.
CC Note=Translocated to the trans-Golgi network area in an OSBP-dependent
CC manner (PubMed:29514919). Colocalizes with RAB11A in recycling
CC endosomes (By similarity). Found in a complex composed of RELCH, OSBP1
CC and RAB11A (By similarity). {ECO:0000250|UniProtKB:Q148V7,
CC ECO:0000269|PubMed:29514919}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P260-2; Sequence=VSP_030016, VSP_030017;
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DR EMBL; AC027514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB040901; BAA95992.1; -; mRNA.
DR CCDS; CCDS11979.2; -. [Q9P260-1]
DR CCDS; CCDS86675.1; -. [Q9P260-2]
DR RefSeq; NP_001333158.1; NM_001346229.1. [Q9P260-2]
DR RefSeq; NP_065905.2; NM_020854.3. [Q9P260-1]
DR AlphaFoldDB; Q9P260; -.
DR BioGRID; 121661; 51.
DR CORUM; Q9P260; -.
DR IntAct; Q9P260; 9.
DR MINT; Q9P260; -.
DR STRING; 9606.ENSP00000381198; -.
DR GlyGen; Q9P260; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P260; -.
DR PhosphoSitePlus; Q9P260; -.
DR BioMuta; KIAA1468; -.
DR DMDM; 166218823; -.
DR EPD; Q9P260; -.
DR jPOST; Q9P260; -.
DR MassIVE; Q9P260; -.
DR MaxQB; Q9P260; -.
DR PaxDb; Q9P260; -.
DR PeptideAtlas; Q9P260; -.
DR PRIDE; Q9P260; -.
DR ProteomicsDB; 83734; -. [Q9P260-1]
DR ProteomicsDB; 83735; -. [Q9P260-2]
DR Antibodypedia; 42133; 50 antibodies from 15 providers.
DR DNASU; 57614; -.
DR Ensembl; ENST00000256858.10; ENSP00000256858.5; ENSG00000134444.15. [Q9P260-2]
DR Ensembl; ENST00000398130.6; ENSP00000381198.2; ENSG00000134444.15. [Q9P260-1]
DR GeneID; 57614; -.
DR KEGG; hsa:57614; -.
DR UCSC; uc002lil.4; human. [Q9P260-1]
DR CTD; 57614; -.
DR DisGeNET; 57614; -.
DR GeneCards; RELCH; -.
DR HGNC; HGNC:29289; RELCH.
DR HPA; ENSG00000134444; Low tissue specificity.
DR MIM; 618001; gene.
DR neXtProt; NX_Q9P260; -.
DR OpenTargets; ENSG00000134444; -.
DR PharmGKB; PA134865247; -.
DR VEuPathDB; HostDB:ENSG00000134444; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00390000004385; -.
DR HOGENOM; CLU_006254_1_0_1; -.
DR InParanoid; Q9P260; -.
DR OMA; RQDLNCA; -.
DR OrthoDB; 73423at2759; -.
DR PhylomeDB; Q9P260; -.
DR TreeFam; TF329740; -.
DR PathwayCommons; Q9P260; -.
DR SignaLink; Q9P260; -.
DR BioGRID-ORCS; 57614; 6 hits in 1082 CRISPR screens.
DR ChiTaRS; RELCH; human.
DR GenomeRNAi; 57614; -.
DR Pharos; Q9P260; Tdark.
DR PRO; PR:Q9P260; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9P260; protein.
DR Bgee; ENSG00000134444; Expressed in esophagus mucosa and 178 other tissues.
DR ExpressionAtlas; Q9P260; baseline and differential.
DR Genevisible; Q9P260; HS.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; IDA: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 SMART; SM00667; LisH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endosome; Golgi apparatus;
KW Lipid transport; Phosphoprotein; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..1216
FT /note="RAB11-binding protein RELCH"
FT /id="PRO_0000313093"
FT DOMAIN 255..287
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 601..639
FT /note="HEAT 1"
FT /evidence="ECO:0000305"
FT REPEAT 640..679
FT /note="HEAT 2"
FT /evidence="ECO:0000305"
FT REPEAT 1004..1042
FT /note="HEAT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00103"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..779
FT /note="Interaction with RAB11A and RAB11B"
FT /evidence="ECO:0000250|UniProtKB:Q148V7"
FT COILED 197..231
FT /evidence="ECO:0000255"
FT COILED 359..397
FT /evidence="ECO:0000255"
FT COMPBIAS 411..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q148V7"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148V7"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148V7"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148V7"
FT VAR_SEQ 920
FT /note="Q -> QIKEYLHIHNEISWEWDPSLNTKCVSYTHYTHSLK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_030016"
FT VAR_SEQ 991..1017
FT /note="TLRGMSEALVDKRVAPALVTLSSDPEF -> LVKGVNETLVAQRVVPALITL
FT SSDPEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_030017"
FT VARIANT 929
FT /note="G -> E (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs770815767)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037660"
SQ SEQUENCE 1216 AA; 134630 MW; 3069B0FFFB00F41D CRC64;
MAAMAPGGSG SGGGVNPFLS DSDEDDDEVA ATEERRAVLR LGAGSGLDPG SAGSLSPQDP
VALGSSARPG LPGEASAAAV ALGGTGETPA RLSIDAIAAQ LLRDQYLLTA LELHTELLES
GRELPRLRDY FSNPGNFERQ SGTPPGMGAP GVPGAAGVGG AGGREPSTAS GGGQLNRAGS
ISTLDSLDFA RYSDDGNRET DEKVAVLEFE LRKAKETIQA LRANLTKAAE HEVPLQERKN
YKSSPEIQEP IKPLEKRALN FLVNEFLLKN NYKLTSITFS DENDDQDFEL WDDVGLNIPK
PPDLLQLYRD FGNHQVTGKD LVDVASGVEE DELEALTPII SNLPPTLETP QPAENSMLVQ
KLEDKISLLN SEKWSLMEQI RRLKSEMDFL KNEHFAIPAV CDSVQPPLDQ LPHKDSEDSG
QHPDVNSSDK GKNTDIHLSI SDEADSTIPK ENSPNSFPRR EREGMPPSSL SSKKTVHFDK
PNRKLSPAFH QALLSFCRMS ADSRLGYEVS RIADSEKSVM LMLGRCLPHI VPNVLLAKRE
ELIPLILCTA CLHPEPKERD QLLHILFNLI KRPDDEQRQM ILTGCVAFAR HVGPTRVEAE
LLPQCWEQIN HKYPERRLLV AESCGALAPY LPKEIRSSLV LSMLQQMLME DKADLVREAV
IKSLGIIMGY IDDPDKYHQG FELLLSALGD PSERVVSATH QVFLPAYAAW TTELGNLQSH
LILTLLNKIE KLLREGEHGL DEHKLHMYLS ALQSLIPSLF ALVLQNAPFS SKAKLHGEVP
QIEVTRFPRP MSPLQDVSTI IGSREQLAVL LQLYDYQLEQ EGTTGWESLL WVVNQLLPQL
IEIVGKINVT STACVHEFSR FFWRLCRTFG KIFTNTKVKP QFQEILRLSE ENIDSSAGNG
VLTKATVPIY ATGVLTCYIQ EEDRKLLVGF LEDVMTLLSL SHAPLDSLKA SFVELGANPA
YHELLLTVLW YGVVHTSALV RCTAARMFEL TLRGMSEALV DKRVAPALVT LSSDPEFSVR
IATIPAFGTI METVIQRELL ERVKMQLASF LEDPQYQDQH SLHTEIIKTF GRVGPNAEPR
FRDEFVIPHL HKLALVNNLQ IVDSKRLDIA THLFEAYSAL SCCFISEDLM VNHFLPGLRC
LRTDMEHLSP EHEVILSSMI KECEQKVENK TVQEPQGSMS IAASLVSEDT KTKFLNKMGQ
LTTSGAMLAN VFQRKK
