MFGM_RAT
ID MFGM_RAT Reviewed; 427 AA.
AC P70490;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Lactadherin;
DE AltName: Full=MFGM;
DE AltName: Full=Milk fat globule-EGF factor 8;
DE Short=MFG-E8;
DE AltName: Full=O-acetyl GD3 ganglioside synthase;
DE Short=AGS;
DE AltName: Full=SED1;
DE Flags: Precursor;
GN Name=Mfge8; Synonyms=Ags;
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 TISSUE=Brain;
RX PubMed=8780713; DOI=10.1006/bbrc.1996.1274;
RA Ogura K., Nara K., Watanabe Y., Kohno K., Tai T., Sanai Y.;
RT "Cloning and expression of cDNA for O-acetylation of GD3 ganglioside.";
RL Biochem. Biophys. Res. Commun. 225:932-938(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 -!- FUNCTION: Contributes to phagocytic removal of apoptotic cells in many
CC tissues. Plays an important role in the maintenance of intestinal
CC epithelial homeostasis and the promotion of mucosal healing. Promotes
CC VEGF-dependent neovascularization (By similarity). Specific ligand for
CC the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to
CC phosphatidylserine-enriched cell surfaces in a receptor-independent
CC manner. Zona pellucida-binding protein which may play a role in gamete
CC interaction. Appears to participate in the O-acetylation of GD3
CC ganglioside sialic acid. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P79385};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P79385}. Secreted
CC {ECO:0000250|UniProtKB:P79385}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome membrane {ECO:0000250|UniProtKB:P79385}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P79385}. Note=Located in the acrosomal
CC region of zona-pellucida bound sperm. {ECO:0000250|UniProtKB:P79385}.
CC -!- TISSUE SPECIFICITY: Spleen, lung, heart, brain and muscle.
CC -!- DOMAIN: The F5/8 type C 2 domain mediates high-affinity binding to
CC phosphatidylserine-containing membranes. {ECO:0000250}.
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DR EMBL; D84068; BAA12210.1; -; mRNA.
DR EMBL; BC085754; AAH85754.1; -; mRNA.
DR PIR; JC4915; JC4915.
DR RefSeq; NP_001035276.1; NM_001040186.2.
DR RefSeq; NP_036943.1; NM_012811.3.
DR AlphaFoldDB; P70490; -.
DR SMR; P70490; -.
DR BioGRID; 247317; 1.
DR IntAct; P70490; 2.
DR GlyGen; P70490; 4 sites.
DR jPOST; P70490; -.
DR PRIDE; P70490; -.
DR GeneID; 25277; -.
DR KEGG; rno:25277; -.
DR UCSC; RGD:3083; rat.
DR CTD; 4240; -.
DR RGD; 3083; Mfge8.
DR VEuPathDB; HostDB:ENSRNOG00000022321; -.
DR HOGENOM; CLU_030066_0_1_1; -.
DR InParanoid; P70490; -.
DR OrthoDB; 441415at2759; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P70490; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017510; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; P70490; baseline and differential.
DR Genevisible; P70490; RN.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0006910; P:phagocytosis, recognition; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEP:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd00057; FA58C; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cell adhesion; Cytoplasmic vesicle; Disulfide bond;
KW EGF-like domain; Fertilization; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..427
FT /note="Lactadherin"
FT /id="PRO_0000007654"
FT DOMAIN 24..61
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 64..108
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 111..267
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 272..427
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT MOTIF 87..89
FT /note="Cell attachment site"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..39
FT /evidence="ECO:0000250"
FT DISULFID 33..49
FT /evidence="ECO:0000250"
FT DISULFID 51..60
FT /evidence="ECO:0000250"
FT DISULFID 68..79
FT /evidence="ECO:0000250"
FT DISULFID 73..96
FT /evidence="ECO:0000250"
FT DISULFID 98..107
FT /evidence="ECO:0000250"
FT DISULFID 111..267
FT /evidence="ECO:0000250"
FT DISULFID 254..258
FT /evidence="ECO:0000250"
FT DISULFID 272..427
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47413 MW; EA8C8631F3EE6047 CRC64;
MQFSRVLAAL CGVLLCASGL FAASGDFCDS SLCLNGGTCL MGQDNDIYCL CPEGFTGLVC
NETEKGPCSP NPCFHDAKCL VTEDTQRGDI FTEYICQCPV GYSGIHCELG CSTKLGLEGG
AIADSQISAS SVYMGFMGLQ RWGPELARLY RTGIVNAWTA SSYDSKPWIQ VDFLRKMRVS
GVMTQGASRA GRAEYLKTFK VAYSLDGRRF EFIQDESGTG DKEFMGNQDN NSLKINMFNP
TLEAQYIRLY PVSCHRGCTL RFELLGCELH GCSEPLGLKN NTIPDSQITA SSSYKTWNLR
AFGWYPHLGR LDNQGKINAW TAQSNSAKEW LQVDLGTQKK VTGIITQGAR DFGHIQYVAS
YKVAHSDDGV QWTVYEEQGT SKVFQGNLDN NSHKKNIFEK PFMARYVRVL PLSWHNRITL
RLELLGC
