HKR1_YEAST
ID HKR1_YEAST Reviewed; 1802 AA.
AC P41809; D6VT50; Q04051;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Signaling mucin HKR1;
DE AltName: Full=Hansenula MRAKII killer toxin-resistant protein 1;
DE Flags: Precursor;
GN Name=HKR1; OrderedLocusNames=YDR420W;
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 [GENOMIC DNA].
RC STRAIN=ATCC 200358 / YNN 295;
RX PubMed=8113191; DOI=10.1128/jb.176.5.1488-1499.1994;
RA Kasahara S., Yamada H., Mio T., Shiratori Y., Miyamoto C., Yabe T.,
RA Nakajima T., Ichishima E., Furuichi Y.;
RT "Cloning of the Saccharomyces cerevisiae gene whose overexpression
RT overcomes the effects of HM-1 killer toxin, which inhibits beta-glucan
RT synthesis.";
RL J. Bacteriol. 176:1488-1499(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8550469; DOI=10.1128/jb.178.2.477-483.1996;
RA Yabe T., Yamada-Okabe T., Kasahara S., Furuichi Y., Nakajima T.,
RA Ichishima E., Arisawa M., Yamada-Okabe H.;
RT "HKR1 encodes a cell surface protein that regulates both cell wall beta-
RT glucan synthesis and budding pattern in the yeast Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 178:477-483(1996).
RN [5]
RP INDUCTION.
RX PubMed=10564805; DOI=10.1111/j.1574-6968.1999.tb08842.x;
RA Braley R., Chaffin W.L.;
RT "Variations in mRNA transcript levels of cell wall-associated genes of
RT Saccharomyces cerevisiae following spheroplasting.";
RL FEMS Microbiol. Lett. 181:177-185(1999).
RN [6]
RP FUNCTION.
RX PubMed=19439450; DOI=10.1091/mbc.e08-07-0760;
RA Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.;
RT "The signaling mucins Msb2 and Hkr1 differentially regulate the
RT filamentation mitogen-activated protein kinase pathway and contribute to a
RT multimodal response.";
RL Mol. Biol. Cell 20:3101-3114(2009).
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: Plasma membrane signaling mucin that promotes activation of
CC the MAPK for the filamentous growth pathway. May regulate beta-glucan
CC synthesis. Overexpression provides resistance to HM-1 killer toxin.
CC {ECO:0000269|PubMed:19439450, ECO:0000269|PubMed:8550469}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8550469};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:8550469}.
CC -!- INDUCTION: Expression is highly increased during spheroplast
CC regeneration. {ECO:0000269|PubMed:10564805}.
CC -!- PTM: Could be O-glycosylated in the serine/threonine-rich domain.
CC -!- SIMILARITY: Belongs to the HKR1/MSB2 family. {ECO:0000305}.
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DR EMBL; S69101; AAB30051.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64857.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12260.1; -; Genomic_DNA.
DR PIR; S69703; S69703.
DR RefSeq; NP_010708.1; NM_001180728.1.
DR AlphaFoldDB; P41809; -.
DR SMR; P41809; -.
DR BioGRID; 32479; 127.
DR IntAct; P41809; 3.
DR MINT; P41809; -.
DR STRING; 4932.YDR420W; -.
DR iPTMnet; P41809; -.
DR PaxDb; P41809; -.
DR PRIDE; P41809; -.
DR EnsemblFungi; YDR420W_mRNA; YDR420W; YDR420W.
DR GeneID; 852030; -.
DR KEGG; sce:YDR420W; -.
DR SGD; S000002828; HKR1.
DR VEuPathDB; FungiDB:YDR420W; -.
DR eggNOG; ENOG502RXIN; Eukaryota.
DR GeneTree; ENSGT01050000245494; -.
DR HOGENOM; CLU_250296_0_0_1; -.
DR InParanoid; P41809; -.
DR OMA; SHISTIM; -.
DR BioCyc; YEAST:G3O-29961-MON; -.
DR PRO; PR:P41809; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P41809; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0005034; F:osmosensor activity; IGI:SGD.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IGI:SGD.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IBA:GO_Central.
DR InterPro; IPR039295; MSB2.
DR PANTHER; PTHR35778; PTHR35778; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1802
FT /note="Signaling mucin HKR1"
FT /id="PRO_0000021444"
FT TOPO_DOM 22..1485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1486..1506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1507..1802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 453..480
FT /note="1; approximate"
FT REPEAT 481..508
FT /note="2"
FT REPEAT 509..536
FT /note="3"
FT REPEAT 537..564
FT /note="4"
FT REPEAT 565..592
FT /note="5"
FT REPEAT 593..620
FT /note="6"
FT REPEAT 621..648
FT /note="7"
FT REPEAT 649..676
FT /note="8"
FT REPEAT 677..704
FT /note="9"
FT REPEAT 705..732
FT /note="10"
FT REPEAT 733..760
FT /note="11"
FT REPEAT 761..788
FT /note="12"
FT REGION 47..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..788
FT /note="12 X 28 AA tandem repeats of S-[AV]-[P]-V-A-V-S-S-T-
FT Y-T-S-S-P-S-A-P-A-A-I-S-S-T-Y-T-S-S-P"
FT REGION 961..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 582
FT /note="V -> A (in Ref. 1; AAB30051)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="V -> A (in Ref. 1; AAB30051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1802 AA; 188948 MW; 0FF726990C7CDC51 CRC64;
MVSLKIKKIL LLVSLLNAIE AYSNDTIYST SYNNGIESTP SYSTSAISST GSSNKENAIT
SSSETTTMAG QYGESGSTTI MDEQETGTSS QYISVTTTTQ TSDTMSSVKK STEIATPSSS
IVPTPLQSYS DESQISQTLS HNPKSVAESD SDTTSSESSS SVIISTSDSS AVPREISPII
TTDSQISKEE GTLAQTSSIS ETTRIAQMVT RVSQISSITA ASTIDGFSSE STQTDFSNTV
SFENSVEEEY AMSKSQLSES YSSSSTVYSG GESTADKTSS SPITSFSSSY SQTTSTETSE
SSRVAVGVSR PSSITQTTSI DSFSMSEVEL STYYDLSAGN YPDQELIVDR PATSSTAETS
SEASQGVSRE SNTFAVSSIS TTNFIVSSAS DTVVSTSSTN TVPYSSVHST FVHATSSSTY
ISSSLYSSPS LSASVSSHFG VAPFPSAYIS FSSVPVAVSS TYTSSPSASV VVPSAYASSP
SVPVAVSSTY TSSPSAPAAI SSTYTSSPSA PVAVSSTYTS SPSAPAAISS TYTSSPSAPV
AVSSTYTSSP SAPAAISSTY TSSPSAPVAV SSTYTSSPSA PVAISSTYTS SPSVPVAVSS
TYTSSPSAPA AISSTYTSSP SAPVAVSSTY TSSPSAPAAI SSTYTSSPSV PVAVSSTYTS
SPSAPAAISS TYTSSPSVPV AVSSTYTSSP SAPAAISSTY TSSPSAPVAV SSTYTSSPSA
PAAISSTYTS SPSAPVAVSS TYTSSPSAPA AISSTYTSSP SAPVAVSSTY TSSPSALVVL
SSTSTSSPYD IVYSPSTFAA ISSGYTPSPS ASVAMSSTSS SSPYDIVYSL SSSASRSSIA
TYEFSPSPST SLPTSSTYTY FSSAYAFEFS SERYSTTSTI APTQIHSTLS RITDFLLQTS
MAIQSIVSQQ ISTSSTLNDE IHSSALSVFN PSASNLVETS LIISSTQASI TSPKNSAKIS
SLQSQLSSST KNPYDTANKN TETSGRSTVV SNFLYTSSAA KPDNEKFSAT PTEITTISSS
SHAYSLSIPS SHNSVTGLSH NFVDSSKSAT SFGYSSSSIS SIKLSKETIP ASKSVSNTQE
RITSFTSTLR ANSQSEKSEG RNSVGSLQSS HISSNPSLST NTKVDSKSLS RKVSKTMGEN
GEETGLTTTK TQYKSSSETS GSYSRSFTKI SIGPATTAVQ TQASTNSVFT APALSTYPTT
PYPSPNSYAW LPTAIIVESS ETGPTTASFN PSITGSLPNA IEPAVAVSEP INHTLITIGF
TAALNYVFLV QNPLSSAQIF NFLPLVLKYP FSNTSSELDN SIGELSTFIL SYRSGSSTTT
LSPKSISSLS VVKKKKNQQK KNATKSTEDL HPPQVDTSSI AVKKIVPMVD SSKAYIVSVA
EVYFPTEAVT YLQQLILDEN STLYSNPQTP LRSLAGLIDS GIPLGGLTLY GSGDGGYVPS
LTSSSVLDSS KGNSQNIDGT YKYGALDDFI NSFTDSASAG KYAVKIIIFL IVLTIGVLLW
LFVAFFAFRH RNILLKRHPR NCIGKSLNNE RELESTELSR SSSGNQVYNE KPPESENESV
YSAVDDHYIV TGENTVYNTI HRLHYTINDD GDLLYRDAIP LDFDQTNGDD GSGIDSIVRD
CVYDKNQDAT EAFLNDEESI SGILDVDENG DIRLYDSYSD NEESNSFHLP DEVIENYNKN
HLCETKLHGL GTESCTTDDP DTGNQITNEF STGSQTCLPS TAYTTPLHTN SIKLHTLRYT
ESSLPKPNQT LFSNLEDLEI EDIDDNGSVS DVHIEELDAL DEELYKRMSK VIKQQNHQTT
KI
