ID M3YC48_MUSPF Unreviewed; 597 AA.
AC M3YC48;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Nephronectin {ECO:0000313|Ensembl:ENSMPUP00000008905.1, ECO:0000313|RefSeq:XP_004748189.1};
GN Name=NPNT {ECO:0000313|Ensembl:ENSMPUP00000008905.1,
GN ECO:0000313|RefSeq:XP_004748189.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000008905.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000008905.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004748189.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004748189.1};
RG RefSeq;
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 EMBL; AEYP01024112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01024113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01024114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004748189.1; XM_004748132.3.
DR STRING; 9669.ENSMPUP00000008905; -.
DR Ensembl; ENSMPUT00000009052.1; ENSMPUP00000008905.1; ENSMPUG00000008978.1.
DR GeneID; 101672509; -.
DR CTD; 255743; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00930000150973; -.
DR HOGENOM; CLU_036867_0_0_1; -.
DR OMA; PETCENE; -.
DR OrthoDB; 19806at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030485; C:smooth muscle contractile fiber; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0097195; P:pilomotor reflex; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; 5.
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; IPR024731; EGF_dom.
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; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 3: Inferred from homology;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041198477"
FT DOMAIN 120..159
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 200..244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 245..285
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 447..590
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 320..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65648 MW; C36ECEAAEE8AF0F6 CRC64;
MDFLLALVLG SSLYLQAAAE FDVRWPRQIV SSVGLCRYGG RIDCCWGWAR RSWGQCQPVC
QPQCKHGECI GPDKCKCHPG YAGKTCNQDE HLYPTPLDQG SEQPLFQPLD HQATSLPSRD
LNECGLKPRP CKHRCMNTYG SYKCYCLNGY MLMPDGSCSS ALTCSMANCQ YGCDVVKGQI
RCQCPSPGLQ LAPDGRTCVD VDECVTGRAS CPRFRQCVNT FGSYVCKCHK GFDLMYIGGK
YQCHDIDECS LGQYQCSRFA RCYNVHGSYK CKCKDGYEGD GLNCVYIPKV MIEPSGPIHV
PKGNGTISKG DGGHSNWIPD VGGTRWPPKT PYIPPVITNR PTSKPTTRPA PRPTPEPTPP
PFPELGTSPP ATSSESTGTQ LTPVVPVVTT SPRWITVDNR IQTDPQKPRG DVFIPRQPSN
DLFEIFEIER GVSADDEAKD DPGVLIHSCN FDHGLCGWIR EKDSDLHWEP VRDPAGGQYL
TVSGAKGPGG KAARLVLPLG HLMHSGDLCL SFRHKVTGLH SGALQVFVRK HGAHGAALWG
RNGGRGWRHT HITLRGADVK SVIFRGEKRR GHTGEIGLDD VSLRKGHCSE ERQRLPN
//
