MRL1_YEAST
ID MRL1_YEAST Reviewed; 381 AA.
AC Q06815; D6W481;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mannose 6-phosphate receptor-like protein 1;
DE Flags: Precursor;
GN Name=MRL1; OrderedLocusNames=YPR079W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11470415; DOI=10.1016/s0960-9822(01)00273-1;
RA Whyte J.R., Munro S.;
RT "A yeast homolog of the mammalian mannose 6-phosphate receptors contributes
RT to the sorting of vacuolar hydrolases.";
RL Curr. Biol. 11:1074-1078(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-339 AND SER-342, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371 AND SER-380, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Sorting receptor involved in the transport of vacuolar
CC enzymes from the Golgi complex to the vacuole. Involved in the delivery
CC and maturation of PEP4 (vacuolar proteinase A) and PRB1 (vacuolar
CC proteinase B). {ECO:0000269|PubMed:11470415}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Single-pass type I membrane protein. Endosome membrane; Single-pass
CC type I membrane protein.
CC -!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}.
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DR EMBL; U51033; AAB68128.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11497.1; -; Genomic_DNA.
DR PIR; S69065; S69065.
DR RefSeq; NP_015404.1; NM_001184176.1.
DR AlphaFoldDB; Q06815; -.
DR SMR; Q06815; -.
DR BioGRID; 36250; 170.
DR DIP; DIP-2873N; -.
DR IntAct; Q06815; 15.
DR MINT; Q06815; -.
DR STRING; 4932.YPR079W; -.
DR iPTMnet; Q06815; -.
DR MaxQB; Q06815; -.
DR PaxDb; Q06815; -.
DR PRIDE; Q06815; -.
DR TopDownProteomics; Q06815; -.
DR EnsemblFungi; YPR079W_mRNA; YPR079W; YPR079W.
DR GeneID; 856194; -.
DR KEGG; sce:YPR079W; -.
DR SGD; S000006283; MRL1.
DR VEuPathDB; FungiDB:YPR079W; -.
DR eggNOG; KOG4504; Eukaryota.
DR HOGENOM; CLU_053195_0_0_1; -.
DR InParanoid; Q06815; -.
DR OMA; KKLTMKY; -.
DR BioCyc; YEAST:G3O-34223-MON; -.
DR PRO; PR:Q06815; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06815; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005048; F:signal sequence binding; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007034; P:vacuolar transport; IMP:SGD.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endosome; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..381
FT /note="Mannose 6-phosphate receptor-like protein 1"
FT /id="PRO_0000042715"
FT TOPO_DOM 24..236
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..230
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 182..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 197..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 381 AA; 42706 MW; 4E89311978E85A4F CRC64;
MLKRSSLIYL SCVLIITIPI LLHVYNGPGL SHEANEHRAS HKQKRTLANP DKPKSENDED
LFCAVTNPVT GSYIDLSQLS STPNKLREGQ KQISGNNKHE SSKTKWSVRG WGYDTNFTLG
ICSSPVGEAE SQQLSNLTGA FYVDQLNENN LVSIGDFSTR PALVGGSTAK KLTLKYENGS
MCPNGKDKKA TLLNFVCDKE IQSKAQISYI GNLHNCSYFF EVRSIHACPT SNKKNEVNVL
GIFIGIFAIF FLVEFAGRRW IYAKLNRHLK NDDELHDISP SLNEQPHWDL IEDGSRWSKF
FNGIIKTTRR FTKSLMRSLV RGRNSRQGGI RLRSSPSASS SSLANREFFR DMEAQNEIID
SLDINSHTTE SDHPTLADNS V
