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LRRN3_RAT
ID   LRRN3_RAT               Reviewed;         707 AA.
AC   Q9ESY6; Q642E4;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Leucine-rich repeat neuronal protein 3;
DE   AltName: Full=Neuronal leucine-rich repeat protein 3;
DE            Short=NLRR-3;
DE   Flags: Precursor;
GN   Name=Lrrn3; Synonyms=Nlrr3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=11549284; DOI=10.1006/bbrc.2001.5579;
RA   Fukamachi K., Matsuoka Y., Kitanaka C., Kuchino Y., Tsuda H.;
RT   "Rat neuronal leucine-rich repeat protein-3: cloning and regulation of the
RT   gene expression.";
RL   Biochem. Biophys. Res. Commun. 287:257-263(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AF291437; AAG00604.1; -; mRNA.
DR   EMBL; BC081791; AAH81791.1; -; mRNA.
DR   PIR; JC7763; JC7763.
DR   RefSeq; NP_110483.1; NM_030856.1.
DR   AlphaFoldDB; Q9ESY6; -.
DR   SMR; Q9ESY6; -.
DR   STRING; 10116.ENSRNOP00000008655; -.
DR   GlyGen; Q9ESY6; 7 sites.
DR   PaxDb; Q9ESY6; -.
DR   GeneID; 81514; -.
DR   KEGG; rno:81514; -.
DR   UCSC; RGD:71066; rat.
DR   CTD; 54674; -.
DR   RGD; 71066; Lrrn3.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q9ESY6; -.
DR   OrthoDB; 998247at2759; -.
DR   PhylomeDB; Q9ESY6; -.
DR   TreeFam; TF334360; -.
DR   PRO; PR:Q9ESY6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030131; C:clathrin adaptor complex; IDA:RGD.
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:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF00041; fn3; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 9.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..707
FT                   /note="Leucine-rich repeat neuronal protein 3"
FT                   /id="PRO_0000045825"
FT   TOPO_DOM        23..626
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        627..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        648..707
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..69
FT                   /note="LRRNT"
FT   REPEAT          70..91
FT                   /note="LRR 1"
FT   REPEAT          93..114
FT                   /note="LRR 2"
FT   REPEAT          117..138
FT                   /note="LRR 3"
FT   REPEAT          141..162
FT                   /note="LRR 4"
FT   REPEAT          165..186
FT                   /note="LRR 5"
FT   REPEAT          189..210
FT                   /note="LRR 6"
FT   REPEAT          213..234
FT                   /note="LRR 7"
FT   REPEAT          237..258
FT                   /note="LRR 8"
FT   REPEAT          261..282
FT                   /note="LRR 9"
FT   REPEAT          285..304
FT                   /note="LRR 10"
FT   REPEAT          310..332
FT                   /note="LRR 11"
FT   REPEAT          335..358
FT                   /note="LRR 12"
FT   DOMAIN          368..421
FT                   /note="LRRCT"
FT   DOMAIN          421..514
FT                   /note="Ig-like C2-type"
FT   DOMAIN          523..614
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        579
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        444..496
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        51
FT                   /note="S -> L (in Ref. 2; AAH81791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="D -> G (in Ref. 2; AAH81791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        656
FT                   /note="N -> S (in Ref. 2; AAH81791)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   707 AA;  79064 MW;  26A210F671EDA875 CRC64;
     MKDAPLQIHV LLGLAITALV QAGDKKVDCP QLCTCEIRPW FTPRSIYMEA STVDCNDLGL
     LNFPARLPAD TQILLLQTNN IARIEHSTDF PVNLTGLDLS QNNLSSVTNI NVQKMSQLLS
     VYLEENKLTE LPEKCLYGLS NLQELYVNHN LLSAISPGAF VGLHNLLRLH LNSNRLQMIN
     SKWFEALPNL EILMLGDNPI LRIKDMNFQP LLKLRSLVIA GINLTEVPDD ALVGLENLES
     ISFYDNRLNK VPQVALQKAV NLKFLDLNKN PINRIRRGDF SNMLHLKELG INNMPELVSI
     DSLAVDNLPD LRKIEATNNP RLSYIHPNAF FRLPKLESLM LNSNALSALY HGTIESLPNL
     KEISIHSNPI RCDCVIRWIN MNKTNIRFME PDSLFCVDPP EFQGQNVRQV HFRDMMEICL
     PLIAPESFPS ILDVEADSYV SLHCRATAEP QPEIYWITPS GKRLLPNTLR EKFYVHSEGT
     LDIRGITPKE GGLYTCIATN LVGADLKSIM IKVGGFVPQD NNGSLNIKIR DIRANSVLVS
     WKANSKILKS SVKWTAFVKT EDSQAAQSAR IPSDVKVYNL THLKPSTEYK ICIDIPTIYQ
     KSRKQCVNVT TKSLEHDGKE NGKSHTVFVA CVGGLLGIIG VMCLFGCVSQ EGNCENEHSY
     TVNHCHKPTL AFSELYPPLI NLWESSKEKP ASLEVKATAI GVPTSMS
 
 
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