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LRC4B_HUMAN
ID   LRC4B_HUMAN             Reviewed;         713 AA.
AC   Q9NT99; Q3ZCQ4; Q58F20;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 3.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Leucine-rich repeat-containing protein 4B;
DE   AltName: Full=Netrin-G3 ligand;
DE            Short=NGL-3;
DE   Flags: Precursor;
GN   Name=LRRC4B; Synonyms=LRIG4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-713.
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 216-636.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
CC   -!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
CC       excitatory synapses. The trans-synaptic adhesion between LRRC4B and
CC       PTPRF regulates the formation of excitatory synapses in a bidirectional
CC       manner (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PTPRF. Interacts with DLG4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC       Presynaptic cell membrane {ECO:0000250}.
CC   -!- DOMAIN: The last 4 C-terminal residues bind to the first 2 PDZ domains
CC       of DLG4. {ECO:0000250}.
CC   -!- PTM: N-glycosylated. O-glycosylated; contains sialic acid.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC008743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019687; AAH19687.1; ALT_INIT; mRNA.
DR   EMBL; BC056207; AAH56207.1; -; mRNA.
DR   EMBL; AL137451; CAB70743.2; -; mRNA.
DR   CCDS; CCDS42595.1; -.
DR   PIR; T46266; T46266.
DR   RefSeq; NP_001073926.1; NM_001080457.1.
DR   RefSeq; NP_001335497.1; NM_001348568.1.
DR   RefSeq; XP_005259486.1; XM_005259429.4.
DR   RefSeq; XP_006723569.1; XM_006723506.3.
DR   RefSeq; XP_011525822.1; XM_011527520.2.
DR   AlphaFoldDB; Q9NT99; -.
DR   SMR; Q9NT99; -.
DR   BioGRID; 125098; 11.
DR   IntAct; Q9NT99; 4.
DR   STRING; 9606.ENSP00000471502; -.
DR   TCDB; 8.A.43.1.24; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR   GlyGen; Q9NT99; 10 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NT99; -.
DR   PhosphoSitePlus; Q9NT99; -.
DR   BioMuta; LRRC4B; -.
DR   DMDM; 91207142; -.
DR   EPD; Q9NT99; -.
DR   MassIVE; Q9NT99; -.
DR   MaxQB; Q9NT99; -.
DR   PaxDb; Q9NT99; -.
DR   PeptideAtlas; Q9NT99; -.
DR   PRIDE; Q9NT99; -.
DR   ProteomicsDB; 82604; -.
DR   Antibodypedia; 53687; 80 antibodies from 18 providers.
DR   DNASU; 94030; -.
DR   Ensembl; ENST00000389201.7; ENSP00000373853.3; ENSG00000131409.13.
DR   Ensembl; ENST00000599957.5; ENSP00000471502.1; ENSG00000131409.13.
DR   Ensembl; ENST00000652263.1; ENSP00000498662.1; ENSG00000131409.13.
DR   GeneID; 94030; -.
DR   KEGG; hsa:94030; -.
DR   MANE-Select; ENST00000652263.1; ENSP00000498662.1; NM_001080457.2; NP_001073926.1.
DR   UCSC; uc002pss.4; human.
DR   CTD; 94030; -.
DR   GeneCards; LRRC4B; -.
DR   HGNC; HGNC:25042; LRRC4B.
DR   HPA; ENSG00000131409; Tissue enhanced (brain, cervix, pituitary gland).
DR   neXtProt; NX_Q9NT99; -.
DR   OpenTargets; ENSG00000131409; -.
DR   PharmGKB; PA134890612; -.
DR   VEuPathDB; HostDB:ENSG00000131409; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000160261; -.
DR   HOGENOM; CLU_000288_18_24_1; -.
DR   InParanoid; Q9NT99; -.
DR   OMA; TSCPEAC; -.
DR   OrthoDB; 282791at2759; -.
DR   PhylomeDB; Q9NT99; -.
DR   TreeFam; TF324303; -.
DR   PathwayCommons; Q9NT99; -.
DR   Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR   SignaLink; Q9NT99; -.
DR   SIGNOR; Q9NT99; -.
DR   BioGRID-ORCS; 94030; 11 hits in 1070 CRISPR screens.
DR   ChiTaRS; LRRC4B; human.
DR   GenomeRNAi; 94030; -.
DR   Pharos; Q9NT99; Tbio.
DR   PRO; PR:Q9NT99; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9NT99; protein.
DR   Bgee; ENSG00000131409; Expressed in cortical plate and 103 other tissues.
DR   ExpressionAtlas; Q9NT99; baseline and differential.
DR   Genevisible; Q9NT99; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0044300; C:cerebellar mossy fiber; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; IBA:GO_Central.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IBA:GO_Central.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
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; IPR026883; LRRC4B.
DR   InterPro; IPR000372; LRRNT.
DR   PANTHER; PTHR24369:SF102; PTHR24369:SF102; 1.
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; 8.
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; 7.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Leucine-rich repeat; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..713
FT                   /note="Leucine-rich repeat-containing protein 4B"
FT                   /id="PRO_0000231654"
FT   TOPO_DOM        36..576
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..713
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          48..86
FT                   /note="LRRNT"
FT   REPEAT          87..108
FT                   /note="LRR 1"
FT   REPEAT          111..132
FT                   /note="LRR 2"
FT   REPEAT          135..156
FT                   /note="LRR 3"
FT   REPEAT          159..180
FT                   /note="LRR 4"
FT   REPEAT          183..205
FT                   /note="LRR 5"
FT   REPEAT          208..229
FT                   /note="LRR 6"
FT   REPEAT          230..251
FT                   /note="LRR 7"
FT   REPEAT          254..275
FT                   /note="LRR 8"
FT   REPEAT          278..299
FT                   /note="LRR 9"
FT   DOMAIN          311..363
FT                   /note="LRRCT"
FT   DOMAIN          364..452
FT                   /note="Ig-like C2-type"
FT   REGION          497..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         693
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C192"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        385..436
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        637..638
FT                   /note="AV -> TA (in Ref. 2; AAH56207)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   713 AA;  76434 MW;  085B5CACE28038D9 CRC64;
     MARARGSPCP PLPPGRMSWP HGALLFLWLF SPPLGAGGGG VAVTSAAGGG SPPATSCPVA
     CSCSNQASRV ICTRRDLAEV PASIPVNTRY LNLQENGIQV IRTDTFKHLR HLEILQLSKN
     LVRKIEVGAF NGLPSLNTLE LFDNRLTTVP TQAFEYLSKL RELWLRNNPI ESIPSYAFNR
     VPSLRRLDLG ELKRLEYISE AAFEGLVNLR YLNLGMCNLK DIPNLTALVR LEELELSGNR
     LDLIRPGSFQ GLTSLRKLWL MHAQVATIER NAFDDLKSLE ELNLSHNNLM SLPHDLFTPL
     HRLERVHLNH NPWHCNCDVL WLSWWLKETV PSNTTCCARC HAPAGLKGRY IGELDQSHFT
     CYAPVIVEPP TDLNVTEGMA AELKCRTGTS MTSVNWLTPN GTLMTHGSYR VRISVLHDGT
     LNFTNVTVQD TGQYTCMVTN SAGNTTASAT LNVSAVDPVA AGGTGSGGGG PGGSGGVGGG
     SGGYTYFTTV TVETLETQPG EEALQPRGTE KEPPGPTTDG VWGGGRPGDA AGPASSSTTA
     PAPRSSRPTE KAFTVPITDV TENALKDLDD VMKTTKIIIG CFVAITFMAA VMLVAFYKLR
     KQHQLHKHHG PTRTVEIINV EDELPAASAV SVAAAAAVAS GGGVGGDSHL ALPALERDHL
     NHHHYVAAAF KAHYSSNPSG GGCGGKGPPG LNSIHEPLLF KSGSKENVQE TQI
 
 
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