RELCH_MOUSE
ID RELCH_MOUSE Reviewed; 1216 AA.
AC Q148V7; Q148V6; Q6PAN5; Q6ZPQ2; Q8C9Z0; Q8CCT3; Q8CD48;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 104.
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 protein containing LisH, coiled-coil, and HEAT repeats {ECO:0000303|PubMed:29514919};
GN Name=Relch; Synonyms=Kiaa1468;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 8-1216 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-20; SER-22; THR-32 AND SER-180, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; THR-183; SER-186;
RP SER-385; SER-792 AND SER-1149, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH RAB11A; RAB11B AND OSBP, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH
RP RAB11A AND OSBP.
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. Functions in membrane tethering and promotes OSBP-
CC mediated cholesterol transfer between RAB11-bound recycling endosomes
CC and OSBP-bound Golgi-like membranes. {ECO:0000250|UniProtKB:Q9P260}.
CC -!- SUBUNIT: Interacts with RAB11A (VIA-GTP form) (PubMed:29514919).
CC Interacts with RAB11B (PubMed:29514919). Interacts (via the third HEAT
CC repeat) with OSBP (via C-terminus) (PubMed:29514919). Found in a
CC complex composed of RELCH, OSBP1 and RAB11A (PubMed:29514919).
CC {ECO:0000269|PubMed:29514919}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:29514919}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9P260}.
CC Note=Colocalization with RAB11A in recycling endosomes
CC (PubMed:29514919). Translocated to the trans-Golgi network area in an
CC OSBP-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9P260,
CC ECO:0000269|PubMed:29514919}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q148V7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q148V7-2; Sequence=VSP_030019;
CC Name=3;
CC IsoId=Q148V7-3; Sequence=VSP_030018, VSP_030020, VSP_030021;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98178.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA.; Evidence={ECO:0000305};
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DR EMBL; AK129368; BAC98178.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK031484; BAC27422.1; -; mRNA.
DR EMBL; AK032147; BAC27723.1; -; mRNA.
DR EMBL; AK040168; BAC30530.1; ALT_INIT; mRNA.
DR EMBL; BC060194; AAH60194.1; -; mRNA.
DR EMBL; BC117949; AAI17950.1; -; mRNA.
DR EMBL; BC117950; AAI17951.1; -; mRNA.
DR CCDS; CCDS15206.1; -. [Q148V7-1]
DR CCDS; CCDS48334.1; -. [Q148V7-2]
DR RefSeq; NP_083625.1; NM_029349.1.
DR RefSeq; NP_775279.2; NM_173187.3.
DR AlphaFoldDB; Q148V7; -.
DR BioGRID; 230627; 5.
DR IntAct; Q148V7; 1.
DR STRING; 10090.ENSMUSP00000039178; -.
DR GlyConnect; 2482; 1 N-Linked glycan (1 site).
DR GlyGen; Q148V7; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q148V7; -.
DR PhosphoSitePlus; Q148V7; -.
DR EPD; Q148V7; -.
DR jPOST; Q148V7; -.
DR MaxQB; Q148V7; -.
DR PaxDb; Q148V7; -.
DR PeptideAtlas; Q148V7; -.
DR PRIDE; Q148V7; -.
DR ProteomicsDB; 269128; -. [Q148V7-1]
DR ProteomicsDB; 269129; -. [Q148V7-2]
DR ProteomicsDB; 269130; -. [Q148V7-3]
DR DNASU; 227446; -.
DR GeneID; 227446; -.
DR KEGG; mmu:227446; -.
DR CTD; 57614; -.
DR MGI; MGI:1922832; Relch.
DR eggNOG; KOG0211; Eukaryota.
DR InParanoid; Q148V7; -.
DR OrthoDB; 73423at2759; -.
DR PhylomeDB; Q148V7; -.
DR BioGRID-ORCS; 227446; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Relch; mouse.
DR PRO; PR:Q148V7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q148V7; protein.
DR GO; GO:0055037; C:recycling endosome; IDA: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 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:17242355"
FT CHAIN 2..1216
FT /note="RAB11-binding protein RELCH"
FT /id="PRO_0000313094"
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..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..779
FT /note="Interaction with RAB11A and RAB11B"
FT /evidence="ECO:0000269|PubMed:29514919"
FT COILED 197..231
FT /evidence="ECO:0000255"
FT COILED 358..397
FT /evidence="ECO:0000255"
FT COMPBIAS 409..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P260"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P260"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P260"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P260"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 78..109
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030018"
FT VAR_SEQ 205..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030019"
FT VAR_SEQ 990..1000
FT /note="LLVKGVNETLV -> VGYIILSCFYL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030020"
FT VAR_SEQ 1001..1216
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030021"
FT CONFLICT 82
FT /note="L -> P (in Ref. 2; BAC27422)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="E -> K (in Ref. 2; BAC27422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="T -> A (in Ref. 2; BAC27422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 134587 MW; AFDC80110D00FA71 CRC64;
MAAMAPGGGG SGSGVNPFLS DSDEDDDEVA ATEDRRAGLR LGAGVGLDPG SAGSLSPQDP
MALGSSARPG LAVEMSAAPA ALGGSGETPA RLSIDAIAAQ LLRDQYLLTA LELHTELLES
GRELPRLRDY FSNPGNFERQ SGTPPGMGAP GIPGASIVGG AGGREPSTTS GGGQLNRAGS
ISTLDSLDFA RYSDDGNRET DERVAVLEFE LRKAKETIQA LRANLTKAAE HEVPLQERKN
YKSSPEIQEP IKPLEKRALN FLVNEFLLKN NYKLTSITFS DENDDQDFEL WDDVGLNIPK
PPDLLQLYRD FGNHQVTGKD LVDVASGVDE DELEALTPIL GNVPPTLDTP LPIENTLLVQ
KLEDKISLLN NEKWSLMEQI RRLESEMDIL KAEHFATPAV GDSVQPSLVW SSQKDSEDNR
QSPAVNSSDQ EKTKDVHLEI PDAADSFIPK ENSSGSFPRK EREELPPSSV SNKTTLHFDQ
PNRKLSPAFH QALLSFCRMS ADSRLGSEVS RIADSEKSVM LMLGRCLPHI VPNVLLAKRE
ELIPLILCTA CLHPEPKERD QLLHILFNLI KRPDDEQRQM ILTGCVAFAR HVGPTRVEAE
LLPQCWEQIN HKYPERRLLV AESCGALAPY LPKEIRSSLV LSMLQQMLME DKADLVREAV
IKSLGIIMGY IDDPDKYQQG FELLLSALGD PSERVVSATH QVFLPAYAAW TTELGNLQSH
LIPTLLNKIE KLLREGEHGL DEHKLHMYLS ALQSLIPSLF ALVLQNAPFS SKAKLHGEVP
HIEVTRFPRP MSPLQDVSTI IGSREQLAVL LQLYDYQLEH EGTTGWESLL WVVNQLLPQL
IEIVGKINVT STACVHEFSR FFWRLCRTFG KIFTNTKVKP QFQEILRLSE ENIDSSAGNG
VLTKATVPIY ATGVLTCYIQ EEDRKLLVGF LEDVMTLLSL SHAPLDSLKA SFVELGANPA
YHELLLTVLW YGVVHTSALV RCTAARMFEL LVKGVNETLV AQRVVPALIT LSSDPEISVR
IATIPAFGTI METVIQRELL ERVKMQLASF LEDPQYQDQH SLHTEVIRTF GRVGPNAEPR
FRDEFVIPHL HKLALVNNLQ IVDSKKLDIA THLFEAYSAL SCCFISEDLM VNHFLPGLRC
LRTDMEHLSP EHEVILSSMI KECEQKVENK TVQEPPGSMS IAASLVSEDT KTKFLNKMGQ
LTTSGAMLAN VFQRKK
