ID D3YTX1_MOUSE Unreviewed; 457 AA.
AC D3YTX1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Nephronectin {ECO:0000313|Ensembl:ENSMUSP00000112816.2};
GN Name=Npnt {ECO:0000313|Ensembl:ENSMUSP00000112816.2,
GN ECO:0000313|MGI:MGI:2148811};
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:0000313|Ensembl:ENSMUSP00000112816.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000112816.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112816.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000112816.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112816.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the nephronectin family.
CC {ECO:0000256|ARBA:ARBA00009738}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; NP_001274032.1; NM_001287103.1.
DR AlphaFoldDB; D3YTX1; -.
DR SMR; D3YTX1; -.
DR MaxQB; D3YTX1; -.
DR PeptideAtlas; D3YTX1; -.
DR ProteomicsDB; 363045; -.
DR Antibodypedia; 1021; 144 antibodies from 23 providers.
DR DNASU; 114249; -.
DR Ensembl; ENSMUST00000117456.8; ENSMUSP00000112816.2; ENSMUSG00000040998.19.
DR GeneID; 114249; -.
DR AGR; MGI:2148811; -.
DR CTD; 255743; -.
DR MGI; MGI:2148811; Npnt.
DR VEuPathDB; HostDB:ENSMUSG00000040998; -.
DR GeneTree; ENSGT00930000150973; -.
DR OrthoDB; 19806at2759; -.
DR BioGRID-ORCS; 114249; 1 hit in 76 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 3.
DR Bgee; ENSMUSG00000040998; Expressed in ascending aorta and 288 other cell types or tissues.
DR ExpressionAtlas; D3YTX1; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000998; MAM_dom.
DR PANTHER; PTHR24050:SF19; NEPHRONECTIN; 1.
DR PANTHER; PTHR24050; PA14 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Proteomics identification {ECO:0007829|MaxQB:D3YTX1,
KW ECO:0007829|PeptideAtlas:D3YTX1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 65..109
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 110..150
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 316..457
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 162..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 50041 MW; 6F85F2C904EDF5EC CRC64;
MNTFGSYKCY CLNGYMLLPD GSCSSALSCS MANCQYGCDV VKGQVRCQCP SPGLQLAPDG
RTCVDIDECA TGRVSCPRFR QCVNTFGSYI CKCHTGFDLM YIGGKYQCHD IDECSLGQHQ
CSSYARCYNI HGSYKCQCRD GYEGDGLNCV YIPKVMIEPS GPIHMPERNG TISKGDGGHA
NRIPDAGSTR WPLKTPYIPP VITNRPTSKP TTRPTPNPTP QPTPPPPPPL PTEPRTTPLP
PTPERPSTRP TTIAPATSTT TRVITVDNRI QTDPQKPRGD VFIPRQPTND LFEIFEIERG
VSADEEVKDD PGILIHSCNF DHGLCGWIRE KDSDLHWETA RDPAGGQYLT VSAAKAPGGK
AARLVLRLGH LMHSGDLCLS FRHKVTGLHS GTLQVFVRKH GTHGAALWGR NGGHGWRQTQ
ITLRGADVKS VIFKGEKRRG HTGEIGLDDV SLKRGRC
//
