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LIGO4_MOUSE
ID   LIGO4_MOUSE             Reviewed;         593 AA.
AC   Q149C3; A0A4X2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Leucine-rich repeat and immunoglobulin-like domain containing-NOGO receptor-interacting protein 4;
DE   AltName: Full=Leucine-rich repeat neuronal protein 6D;
DE   Flags: Precursor;
GN   Name=Lingo4; Synonyms=Lrrn6d;
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 [LARGE SCALE MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-401.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI17867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI17868.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC31214.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC117866; AAI17867.1; ALT_INIT; mRNA.
DR   EMBL; BC117867; AAI17868.1; ALT_INIT; mRNA.
DR   EMBL; AK042286; BAC31214.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS17592.1; -.
DR   RefSeq; NP_796224.1; NM_177250.2.
DR   AlphaFoldDB; Q149C3; -.
DR   SMR; Q149C3; -.
DR   BioGRID; 236263; 1.
DR   STRING; 10090.ENSMUSP00000058050; -.
DR   GlyGen; Q149C3; 6 sites.
DR   iPTMnet; Q149C3; -.
DR   PhosphoSitePlus; Q149C3; -.
DR   PaxDb; Q149C3; -.
DR   PRIDE; Q149C3; -.
DR   ProteomicsDB; 252475; -.
DR   DNASU; 320747; -.
DR   GeneID; 320747; -.
DR   KEGG; mmu:320747; -.
DR   UCSC; uc008qgb.1; mouse.
DR   CTD; 339398; -.
DR   MGI; MGI:2444651; Lingo4.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q149C3; -.
DR   OrthoDB; 428840at2759; -.
DR   PhylomeDB; Q149C3; -.
DR   TreeFam; TF334360; -.
DR   BioGRID-ORCS; 320747; 2 hits in 71 CRISPR screens.
DR   PRO; PR:Q149C3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q149C3; protein.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
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   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; PF07679; I-set; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 10.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 8.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Leucine-rich repeat;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..593
FT                   /note="Leucine-rich repeat and immunoglobulin-like domain
FT                   containing-NOGO receptor-interacting protein 4"
FT                   /id="PRO_0000324185"
FT   TOPO_DOM        30..533
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        555..593
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..60
FT                   /note="LRRNT"
FT   REPEAT          61..82
FT                   /note="LRR 1"
FT   REPEAT          85..106
FT                   /note="LRR 2"
FT   REPEAT          109..130
FT                   /note="LRR 3"
FT   REPEAT          133..154
FT                   /note="LRR 4"
FT   REPEAT          157..178
FT                   /note="LRR 5"
FT   REPEAT          181..202
FT                   /note="LRR 6"
FT   REPEAT          210..231
FT                   /note="LRR 7"
FT   REPEAT          253..274
FT                   /note="LRR 8"
FT   REPEAT          277..298
FT                   /note="LRR 9"
FT   REPEAT          301..322
FT                   /note="LRR 10"
FT   REPEAT          325..346
FT                   /note="LRR 11"
FT   DOMAIN          358..412
FT                   /note="LRRCT"
FT   DOMAIN          412..502
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        435..484
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   593 AA;  64189 MW;  CCF153432BE07A5B CRC64;
     MDAATAPKQA WLPWSPLLFL LLLPGGSISS CPTVCDCTSQ TRAVFCAHRR LDTIPGGLPL
     DTELLDLSGN RLWGLQRGML SRLGQLQELD LSYNQLSTLE PGAFHGLQSL LTLRLQGNRL
     RIVGPGIFSG LTALTLLDLR LNQIVLFLDG AFSELGSLQQ LEVGDNHLVF VAPGAFAGLA
     KLSTITLERC NLSTVPGLAL AQLPALVALR LRELDIERLP AGALRGLGQL KELEIHHWPS
     LEALDPGSLV GLNLSSLAIT RCNLSSVPFQ ALHHLSFLRI LDLSQNPISA IPARRLSPLV
     RLQELRLSGA CLTSIAAHAF HGLTAFHLLD VADNALQTLE ETAFPSPDKL VTLRLSGNPL
     TCDCRLLWLL RLRRRLDFGT SPPACAGPQH VQGKSLREFS DILPPGHFTC KPALIRKSGP
     RWVIAEEGGH AVFSCSGDGD PAPTVSWMRP QGAWLGRVGR VRVLEDGTLE IRSVQLRDRG
     AYVCVVSNVA GNDSLRTWLE VIQVEPPNGT LSDPNITMPG IPGPFFLDSR GVAMVLAVGF
     LPFLTSVTLC FGLIALWSKG KGRVKHHMTF DFVAPRPSGD KNSGGNRVTA KLF
 
 
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