TRE2_YEAST
ID TRE2_YEAST Reviewed; 809 AA.
AC Q08693; D6W2V7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative zinc metalloprotease TRE2;
DE EC=3.-.-.-;
DE AltName: Full=Transferrin receptor-like protein 2;
GN Name=TRE2; OrderedLocusNames=YOR256C;
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 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; Z75164; CAA99478.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11023.1; -; Genomic_DNA.
DR PIR; S67153; S67153.
DR RefSeq; NP_014899.1; NM_001183675.2.
DR AlphaFoldDB; Q08693; -.
DR SMR; Q08693; -.
DR BioGRID; 34646; 23.
DR IntAct; Q08693; 1.
DR STRING; 4932.YOR256C; -.
DR TCDB; 9.B.229.1.7; the transferrin receptor, cd71, (tfr) family.
DR iPTMnet; Q08693; -.
DR MaxQB; Q08693; -.
DR PaxDb; Q08693; -.
DR PRIDE; Q08693; -.
DR TopDownProteomics; Q08693; -.
DR EnsemblFungi; YOR256C_mRNA; YOR256C; YOR256C.
DR GeneID; 854430; -.
DR KEGG; sce:YOR256C; -.
DR SGD; S000005782; TRE2.
DR VEuPathDB; FungiDB:YOR256C; -.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR HOGENOM; CLU_005688_1_1_1; -.
DR InParanoid; Q08693; -.
DR OMA; IGRRQCK; -.
DR BioCyc; YEAST:G3O-33747-MON; -.
DR Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:Q08693; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08693; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IGI:SGD.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..809
FT /note="Putative zinc metalloprotease TRE2"
FT /id="PRO_0000237639"
FT TOPO_DOM 1..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..809
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 255..349
FT /note="PA"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 809 AA; 91995 MW; D7D68C0A8C50ECB2 CRC64;
MRSSYQPVST TNFEHENAIP TASSSHNLLM SQRFDDSPPS SNDNSIETNI TPPPEPPSYE
FDIEDPHDDL HKRTHLQRVS IGFQEKILEP LMENIIHPLL QISKFVPDKA DYYLSKIGNP
FILRRFFYII FMSFIAYYVL SSGYLFNEKA SGSKGMFSQH DILFEYAKKS VDLAKFERDL
EYISSMPHGS GTKGDAAIYR YIQESFDNNG LKLVKEMGYS VYSNYPGNVS ISYYDNKNEK
HDLELSKENF NPLSSNGKLS KVSLIYGGKG TTYDLQHLKD SKTIEDGKDY VLLLQYDKLV
SQQVLIAEKF GAKAVIFISE PYGENIDVVQ SKPVGLPQYS TGDASGLNWD GSPVEEKDHK
FWRQTHIPTI PISTRQGKEL LSRLSSGGVT VDDGNSDRSN SGKMGDVLID VDLQTNVREK
HFIPNIVGKI EGREQSDKAI IIAASRNSIN FGTTYPNFGT AALLSIVQLF QEVKYKFGWK
PLRNIYFISF GGTEFNYAGS SELVEQRLTP LKDEIYSLID ISQLGIPFAE KYENGKTRGE
LSIETHPLLK KFFNRNAHGN FDISVDNVQH YGDWTPFLAN GIPVSVISSD STRNRDTPTE
TSEDKFERVE KILEDEQNQQ SVKDLLVYLL HISMELIDDP LLHFDIISYV EDIDERLQRL
EQAYPEKLNF TSIIKGLLFW KKIGSEWASW TQGWENIVWS HGDGIEPSLL SINRWTWNKK
LTNIGRRTCS PAGLPNRSFY KNVLFGPTLI QEDKSKNGGN VDFWTFPGVM DAIYDDDWKR
AQEQIDLIGK VLHQSAALFV EETNDIGYK
