NOP1_NEUCR
ID NOP1_NEUCR Reviewed; 304 AA.
AC Q9UW81; Q7RVS2;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Opsin-1;
DE AltName: Full=NR;
GN Name=nop-1; ORFNames=NCU10055;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=10393943; DOI=10.1073/pnas.96.14.8034;
RA Bieszke J.A., Braun E.L., Bean L.E., Kang S., Natvig D.O., Borkovich K.A.;
RT "The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix
RT retinal-binding protein homologous to archaeal rhodopsins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8034-8039(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3] {ECO:0000305}
RP RETINAL-BINDING.
RX PubMed=10571987; DOI=10.1021/bi9916170;
RA Bieszke J.A., Spudich E.N., Scott K.L., Borkovich K.A., Spudich J.L.;
RT "A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-
RT like photochemically reactive pigment.";
RL Biochemistry 38:14138-14145(1999).
RN [4] {ECO:0000305}
RP MUTAGENESIS OF ASP-131 AND GLU-142, AND FOURIER-TRANSFORM INFRARED
RP SPECTROSCOPY.
RX PubMed=11435422; DOI=10.1074/jbc.m102652200;
RA Brown L.S., Dioumaev A.K., Lanyi J.K., Spudich E.N., Spudich J.L.;
RT "Photochemical reaction cycle and proton transfers in Neurospora
RT rhodopsin.";
RL J. Biol. Chem. 276:32495-32505(2001).
RN [5] {ECO:0000305}
RP FOURIER-TRANSFORM INFRARED SPECTROSCOPY OF WILD-TYPE AND MUTANT GLU-131.
RX PubMed=12403457; DOI=10.1562/0031-8655(2002)076<0341:aftiso>2.0.co;2;
RA Bergo V., Spudich E.N., Spudich J.L., Rothschild K.J.;
RT "A Fourier transform infrared study of Neurospora rhodopsin: similarities
RT with archaeal rhodopsins.";
RL Photochem. Photobiol. 76:341-349(2002).
CC -!- FUNCTION: Could facilitate a sensory photoresponse.
CC {ECO:0000303|PubMed:10571987, ECO:0000303|PubMed:12403457}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highest expression in sexually differentiated
CC cultures and conidia when there has been exposure to light. Also
CC expressed during vegetative growth. {ECO:0000269|PubMed:10393943}.
CC -!- PTM: Binds all-trans retinal via a protonated Schiff base linkage.
CC {ECO:0000269|PubMed:10393943, ECO:0000269|PubMed:10571987}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; AF135863; AAD45253.1; -; Genomic_DNA.
DR EMBL; CM002242; EAA30185.1; -; Genomic_DNA.
DR RefSeq; XP_959421.1; XM_954328.3.
DR AlphaFoldDB; Q9UW81; -.
DR SMR; Q9UW81; -.
DR STRING; 5141.EFNCRP00000009817; -.
DR TCDB; 3.E.1.4.2; the ion-translocating microbial rhodopsin (mr) family.
DR EnsemblFungi; EAA30185; EAA30185; NCU10055.
DR GeneID; 3875568; -.
DR KEGG; ncr:NCU10055; -.
DR VEuPathDB; FungiDB:NCU10055; -.
DR HOGENOM; CLU_054785_0_0_1; -.
DR OMA; VCRQVFW; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005503; F:all-trans retinal binding; IDA:UniProtKB.
DR GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009416; P:response to light stimulus; NAS:UniProtKB.
DR InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR InterPro; IPR018229; Rhodopsin_retinal_BS.
DR PANTHER; PTHR28286; PTHR28286; 1.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR PRINTS; PR00251; BACTRLOPSIN.
DR SMART; SM01021; Bac_rhodopsin; 1.
DR PROSITE; PS00950; BACTERIAL_OPSIN_1; 1.
DR PROSITE; PS00327; BACTERIAL_OPSIN_RET; 1.
PE 1: Evidence at protein level;
KW Chromophore; Membrane; Photoreceptor protein; Receptor; Reference proteome;
KW Retinal protein; Schiff base; Sensory transduction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..304
FT /note="Opsin-1"
FT /id="PRO_0000196283"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 263
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 131
FT /note="D->E: Changes in photocycle indicate that this
FT residue is involved in reprotonation of the Schiff-base."
FT /evidence="ECO:0000269|PubMed:11435422"
FT MUTAGEN 142
FT /note="E->Q: Little change in photocycle, indicating that
FT this residue is not involved in reprotonation of the
FT Schiff-base."
FT /evidence="ECO:0000269|PubMed:11435422"
SQ SEQUENCE 304 AA; 33487 MW; CEF1266CAC67F6D9 CRC64;
MIHPEQVADM LRPTTSTTSS HVPGPVPTVV PTPTEYQTLG ETGHRTLWVT FALMVLSSGI
FALLSWNVPT SKRLFHVITT LITVVASLSY FAMATGHATT FNCDTAWDHH KHVPDTSHQV
CRQVFWGRYV DWALTTPLLL LELCLLAGVD GAHTLMAIVA DVIMVLCGLF AALGEGGNTA
QKWGWYTIGC FSYLFVIWHV ALHGSRTVTA KGRGVSRLFT GLAVFALLLW TAYPIIWGIA
GGARRTNVDT EILIYTVLDL LAKPVFGFWL LLSHRAMPET NIDLPGYWSH GLATEGRIRI
GEED
