HIP1_YEAST
ID HIP1_YEAST Reviewed; 603 AA.
AC P06775; D6VUX3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Histidine permease;
GN Name=HIP1; OrderedLocusNames=YGR191W; ORFNames=G7572;
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].
RX PubMed=3905514; DOI=10.1016/0378-1119(85)90219-7;
RA Tanaka J., Fink G.R.;
RT "The histidine permease gene (HIP1) of Saccharomyces cerevisiae.";
RL Gene 38:205-214(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7645350; DOI=10.1002/yea.320110609;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
RT "The complete sequence of a 9037 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 11:587-591(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [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).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76, AND IDENTIFICATION BY
RP 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: High-affinity permease for histidine.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; M11980; AAA34673.1; -; Genomic_DNA.
DR EMBL; X82408; CAA57802.1; -; Genomic_DNA.
DR EMBL; Z72975; CAA97217.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08284.1; -; Genomic_DNA.
DR PIR; S55869; S55869.
DR RefSeq; NP_011707.1; NM_001181320.1.
DR AlphaFoldDB; P06775; -.
DR SMR; P06775; -.
DR BioGRID; 33444; 26.
DR DIP; DIP-5549N; -.
DR IntAct; P06775; 3.
DR MINT; P06775; -.
DR STRING; 4932.YGR191W; -.
DR TCDB; 2.A.3.10.1; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P06775; -.
DR SwissPalm; P06775; -.
DR MaxQB; P06775; -.
DR PaxDb; P06775; -.
DR PRIDE; P06775; -.
DR EnsemblFungi; YGR191W_mRNA; YGR191W; YGR191W.
DR GeneID; 853104; -.
DR KEGG; sce:YGR191W; -.
DR SGD; S000003423; HIP1.
DR VEuPathDB; FungiDB:YGR191W; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; P06775; -.
DR OMA; KINSDAW; -.
DR BioCyc; YEAST:G3O-30880-MON; -.
DR PRO; PR:P06775; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P06775; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005291; F:high-affinity L-histidine transmembrane transporter activity; IMP:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015817; P:histidine transport; IMP:SGD.
DR GO; GO:0006828; P:manganese ion transport; IMP:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..603
FT /note="Histidine permease"
FT /id="PRO_0000054154"
FT TOPO_DOM 1..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 45..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 603 AA; 66006 MW; 77DD34F1DA95E75F CRC64;
MPRNPLKKEY WADVVDGFKP ATSPAFENEK ESTTFVTELT SKTDSAFPLS SKDSPGINQT
TNDITSSDRF RRNEDTEQED INNTNLSKDL SVRHLLTLAV GGAIGTGLYV NTGAALSTGG
PASLVIDWVI ISTCLFTVIN SLGELSAAFP VVGGFNVYSM RFIEPSFAFA VNLNYLAQWL
VLLPLELVAA SITIKYWNDK INSDAWVAIF YATIALANML DVKSFGETEF VLSMIKILSI
IGFTILGIVL SCGGGPHGGY IGGKYWHDPG AFVGHSSGTQ FKGLCSVFVT AAFSYSGIEM
TAVSAAESKN PRETIPKAAK RTFWLITASY VTILTLIGCL VPSNDPRLLN GSSSVDAASS
PLVIAIENGG IKGLPSLMNA IILIAVVSVA NSAVYACSRC MVAMAHIGNL PKFLNRVDKR
GRPMNAILLT LFFGLLSFVA ASDKQAEVFT WLSALSGLST IFCWMAINLS HIRFRQAMKV
QERSLDELPF ISQTGVKGSW YGFIVLFLVL IASFWTSLFP LGGSGASAES FFEGYLSFPI
LIVCYVGHKL YTRNWTLMVK LEDMDLDTGR KQVDLTLRRE EMRIERETLA KRSFVTRFLH
FWC
