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NEGR1_MOUSE
ID   NEGR1_MOUSE             Reviewed;         348 AA.
AC   Q80Z24; Q3UHQ8; Q80T70;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Neuronal growth regulator 1;
DE   AltName: Full=Kindred of IgLON;
DE            Short=Kilon;
DE   AltName: Full=Neurotractin;
DE   Flags: Precursor;
GN   Name=Negr1; Synonyms=Kiaa3001, Ntra;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=15946856; DOI=10.1016/j.mcn.2005.04.010;
RA   Schaefer M., Braeuer A.U., Savaskan N.E., Rathjen F.G., Bruemmendorf T.;
RT   "Neurotractin/kilon promotes neurite outgrowth and is expressed on reactive
RT   astrocytes after entorhinal cortex lesion.";
RL   Mol. Cell. Neurosci. 29:580-590(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-348.
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Brown adipose tissue;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in cell-adhesion. May function as a trans-
CC       neural growth-promoting factor in regenerative axon sprouting in the
CC       mammalian brain. {ECO:0000269|PubMed:15946856}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:15946856}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC       {ECO:0000305}.
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DR   EMBL; AJ487032; CAD31699.1; -; mRNA.
DR   EMBL; AK142298; BAE25018.1; -; mRNA.
DR   EMBL; AK147253; BAE27799.1; -; mRNA.
DR   EMBL; AK122576; BAC65858.2; -; mRNA.
DR   CCDS; CCDS17930.1; -.
DR   RefSeq; NP_001034183.1; NM_001039094.3.
DR   RefSeq; NP_796248.1; NM_177274.4.
DR   AlphaFoldDB; Q80Z24; -.
DR   SMR; Q80Z24; -.
DR   BioGRID; 236331; 21.
DR   IntAct; Q80Z24; 1.
DR   MINT; Q80Z24; -.
DR   STRING; 10090.ENSMUSP00000073664; -.
DR   GlyConnect; 2550; 7 N-Linked glycans (4 sites).
DR   GlyGen; Q80Z24; 6 sites, 7 N-linked glycans (4 sites).
DR   iPTMnet; Q80Z24; -.
DR   PhosphoSitePlus; Q80Z24; -.
DR   MaxQB; Q80Z24; -.
DR   PaxDb; Q80Z24; -.
DR   PeptideAtlas; Q80Z24; -.
DR   PRIDE; Q80Z24; -.
DR   ProteomicsDB; 252878; -.
DR   Antibodypedia; 2206; 203 antibodies from 29 providers.
DR   DNASU; 320840; -.
DR   Ensembl; ENSMUST00000074015; ENSMUSP00000073664; ENSMUSG00000040037.
DR   GeneID; 320840; -.
DR   KEGG; mmu:320840; -.
DR   UCSC; uc008rvc.2; mouse.
DR   CTD; 257194; -.
DR   MGI; MGI:2444846; Negr1.
DR   VEuPathDB; HostDB:ENSMUSG00000040037; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000159289; -.
DR   HOGENOM; CLU_027228_2_3_1; -.
DR   InParanoid; Q80Z24; -.
DR   OMA; CLAISME; -.
DR   OrthoDB; 583722at2759; -.
DR   PhylomeDB; Q80Z24; -.
DR   TreeFam; TF351104; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 320840; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Negr1; mouse.
DR   PRO; PR:Q80Z24; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q80Z24; protein.
DR   Bgee; ENSMUSG00000040037; Expressed in piriform cortex and 191 other tissues.
DR   ExpressionAtlas; Q80Z24; baseline and differential.
DR   Genevisible; Q80Z24; MM.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR   GO; GO:0007631; P:feeding behavior; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IDA:MGI.
DR   GO; GO:0051963; P:regulation of synapse assembly; ISO:MGI.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..318
FT                   /note="Neuronal growth regulator 1"
FT                   /id="PRO_0000015039"
FT   PROPEP          319..348
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015040"
FT   DOMAIN          32..128
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          133..215
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          219..307
FT                   /note="Ig-like C2-type 3"
FT   MOD_RES         181
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   LIPID           318
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3B1"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        154..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        239..291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   348 AA;  37900 MW;  30520A146A9FA198 CRC64;
     MVLLAQGACC SNQWLAAVLL SLCSCLPAGQ SVDFPWAAVD NMLVRKGDTA VLRCYLEDGA
     SKGAWLNRSS IIFAGGDKWS VDPRVSISTL NKRDYSLQIQ NVDVTDDGPY TCSVQTQHTP
     RTMQVHLTVQ VPPKIYDISN DMTINEGTNV TLTCLATGKP EPVISWRHIS PSAKPFENGQ
     YLDIYGITRD QAGEYECSAE NDVSFPDVKK VRVIVNFAPT IQEIKSGTVT PGRSGLIRCE
     GAGVPPPAFE WYKGEKRLFN GQQGIIIQNF STRSILTVTN VTQEHFGNYT CVAANKLGTT
     NASLPLNPPS TAQYGITGSA CDLFSCWSLA LTLSSVISIF YLKNAILQ
 
 
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