NYX_MOUSE
ID NYX_MOUSE Reviewed; 476 AA.
AC P83503; Q8BYN4;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Nyctalopin;
DE Flags: Precursor;
GN Name=Nyx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH35244.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DISEASE.
RX PubMed=12506099; DOI=10.1167/iovs.02-0501;
RA Gregg R.G., Mukhopadhyay S., Candille S.I., Ball S.L., Pardue M.T.,
RA McCall M.A., Peachey N.S.;
RT "Identification of the gene and the mutation responsible for the mouse nob
RT phenotype.";
RL Invest. Ophthalmol. Vis. Sci. 44:378-384(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=12714669; DOI=10.1167/iovs.02-0115;
RA Pesch K., Zeitz C., Fries J.E., Muenscher S., Pusch C.M., Kohler K.,
RA Berger W., Wissinger B.;
RT "Isolation of the mouse nyctalopin gene Nyx and expression studies in mouse
RT and rat retina.";
RL Invest. Ophthalmol. Vis. Sci. 44:2260-2266(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-343.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in retina with lower levels in
CC brain, lung, spleen and testis. Not detected in kidney, heart or liver.
CC In the retina, highest expression found in the inner nuclear layer and
CC ganglion cell layer. {ECO:0000269|PubMed:12506099,
CC ECO:0000269|PubMed:12714669}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all stages of postnatal retinal
CC development. {ECO:0000269|PubMed:12714669}.
CC -!- DISEASE: Note=Defects in Nyx are the cause of the nob (no b-wave)
CC phenotype which is characterized by a decreased sensitivity to light
CC and an absence of the rod b-wave in electroretinograms. An 85-bp
CC deletion in exon 3 results in the loss of 288 residues from the C-
CC terminus of the protein. {ECO:0000269|PubMed:12506099}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class IV subfamily. {ECO:0000305}.
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DR EMBL; AY114303; AAM47034.1; -; mRNA.
DR EMBL; BC035244; AAH35244.1; -; mRNA.
DR EMBL; BC048381; AAH48381.1; -; mRNA.
DR EMBL; AK038912; BAC30165.1; -; mRNA.
DR CCDS; CCDS40877.1; -.
DR RefSeq; NP_775591.1; NM_173415.4.
DR RefSeq; XP_006527675.1; XM_006527612.3.
DR RefSeq; XP_006527676.1; XM_006527613.3.
DR RefSeq; XP_006527677.1; XM_006527614.3.
DR AlphaFoldDB; P83503; -.
DR SMR; P83503; -.
DR STRING; 10090.ENSMUSP00000056313; -.
DR GlyGen; P83503; 7 sites.
DR iPTMnet; P83503; -.
DR PhosphoSitePlus; P83503; -.
DR PaxDb; P83503; -.
DR PRIDE; P83503; -.
DR ProteomicsDB; 294259; -.
DR Antibodypedia; 55948; 99 antibodies from 16 providers.
DR Ensembl; ENSMUST00000050434; ENSMUSP00000056313; ENSMUSG00000051228.
DR GeneID; 236690; -.
DR KEGG; mmu:236690; -.
DR UCSC; uc009srn.1; mouse.
DR CTD; 60506; -.
DR MGI; MGI:2448607; Nyx.
DR VEuPathDB; HostDB:ENSMUSG00000051228; -.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000160782; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; P83503; -.
DR OMA; RSPEGYC; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P83503; -.
DR TreeFam; TF337463; -.
DR BioGRID-ORCS; 236690; 2 hits in 72 CRISPR screens.
DR PRO; PR:P83503; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P83503; protein.
DR Bgee; ENSMUSG00000051228; Expressed in retinal neural layer and 34 other tissues.
DR Genevisible; P83503; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
PE 2: Evidence at transcript level;
KW Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Sensory transduction; Signal; Vision.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..476
FT /note="Nyctalopin"
FT /id="PRO_0000032777"
FT DOMAIN 19..57
FT /note="LRRNT"
FT REPEAT 58..79
FT /note="LRR 1"
FT REPEAT 82..103
FT /note="LRR 2"
FT REPEAT 106..128
FT /note="LRR 3"
FT REPEAT 131..154
FT /note="LRR 4"
FT REPEAT 155..177
FT /note="LRR 5"
FT REPEAT 178..199
FT /note="LRR 6"
FT REPEAT 202..223
FT /note="LRR 7"
FT REPEAT 226..247
FT /note="LRR 8"
FT REPEAT 250..271
FT /note="LRR 9"
FT REPEAT 274..295
FT /note="LRR 10"
FT REPEAT 298..319
FT /note="LRR 11"
FT DOMAIN 331..383
FT /note="LRRCT"
FT CARBOHYD 92
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 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 52431 MW; AF575C25638BC410 CRC64;
MLILLLHAVV FSLPYTRATE ACLRACPAAC TCSHVERGCS VRCDRAGLQR VPQEFPCEAA
SIDLDRNGLR ILGERAFGTL PSLRRLSLRH NNLSFITPGA FKGLPRLAEL RLAHNGELRY
LHVRTFAALG RLRRLDLAAC RLFSVPERLL AELPALRELT AFDNLFRRVP GALRGLANLT
HAHFERSRIE AVASGSLLGM RRLRSLSLQA NRVRAVHAGA FGDCGALEDL LLNDNLLATL
PAAAFRGLRR LRTLNLGGNA LGSVARAWFS DLAELELLYL DRNSITFVEE GAFQNLSGLL
ALHLNGNRLT VLSWAAFQPG FFLGRLFLFR NPWRCDCQLE WLRDWMEGSG RVADVACASP
GSVAGQDLSQ VVFERSSDGL CVDPDELNFT TSSPGPSPEP VATTVSRFSS LLSKLLAPRA
PVEEVANTTW ELVNVSLNDS FRSHAVMVFC YKATFLFTSC VLLSLAQYVV VGLQRE
