MFGM_PIG
ID MFGM_PIG Reviewed; 409 AA.
AC P79385;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Lactadherin;
DE AltName: Full=MFGM;
DE AltName: Full=Milk fat globule-EGF factor 8;
DE Short=MFG-E8;
DE AltName: Full=SED1;
DE AltName: Full=Sperm surface protein SP47;
DE Short=PP47;
GN Name=MFGE8;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-13; 203-214; 267-291;
RP 343-349 AND 378-402, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9546740; DOI=10.1095/biolreprod58.4.1057;
RA Ensslin M.A., Vogel T., Calvete J.J., Thole H.H., Schmidtke J., Matsuda T.,
RA Toepfer-Petersen E.;
RT "Molecular cloning and characterization of P47, a novel boar sperm-
RT associated zona pellucida-binding protein homologous to a family of
RT mammalian secretory proteins.";
RL Biol. Reprod. 58:1057-1064(1998).
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. {ECO:0000250, ECO:0000269|PubMed:9546740}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9546740}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9546740}. Secreted
CC {ECO:0000269|PubMed:9546740}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome membrane {ECO:0000305|PubMed:9546740}; Peripheral membrane
CC protein {ECO:0000305|PubMed:9546740}. Note=Located in the acrosomal
CC region of zona-pellucida bound sperm.
CC -!- TISSUE SPECIFICITY: Mammary epithelial cell surfaces and spermatozoan.
CC Also present in testis, epididymis, uterus, adrenal gland, tonsil,
CC muscle, heart, lymphatic gland, thymus and kidney but not spleen,
CC liver, lung or brain. {ECO:0000269|PubMed:9546740}.
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; Y11683; CAA72379.1; -; mRNA.
DR PIR; T11743; T11743.
DR AlphaFoldDB; P79385; -.
DR SMR; P79385; -.
DR STRING; 9823.ENSSSCP00000002007; -.
DR PaxDb; P79385; -.
DR PeptideAtlas; P79385; -.
DR PRIDE; P79385; -.
DR eggNOG; ENOG502RXUZ; Eukaryota.
DR InParanoid; P79385; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Angiogenesis; Cell adhesion; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Fertilization;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Secreted.
FT CHAIN 1..409
FT /note="Lactadherin"
FT /id="PRO_0000055633"
FT DOMAIN 2..41
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 44..88
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 91..247
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 252..409
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT MOTIF 67..69
FT /note="Cell attachment site"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 6..17
FT /evidence="ECO:0000250"
FT DISULFID 11..29
FT /evidence="ECO:0000250"
FT DISULFID 31..40
FT /evidence="ECO:0000250"
FT DISULFID 48..59
FT /evidence="ECO:0000250"
FT DISULFID 53..76
FT /evidence="ECO:0000250"
FT DISULFID 78..87
FT /evidence="ECO:0000250"
FT DISULFID 91..247
FT /evidence="ECO:0000250"
FT DISULFID 234..238
FT /evidence="ECO:0000250"
FT DISULFID 252..409
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 45725 MW; B0C07AF80029927A CRC64;
FSGDFCDSSL CLNGGTCLLD QDPQKPFHCL CPEGFTGLIC NETEKGPCFP NPCHNDAECE
VIDDAHRGDV FTEYICKCPH GYTGIHCEII CNAPLGMETG AIADFQISAS SMHLGFMGLQ
RWAPELARLH RAGIVNAWTA SNYDRNPWIQ VNLLRRMRVT GVVTQGASRA GSAEYMKTFK
VAYSTDGRKF QFIQGAEESG DKIFMGNLDN SGLKVNLFEV PLEVQYVRLV PIICHRGCTL
RFELLGCELS GCAEPLGLKD NTIPNKQITA SSFYRTWGLS AFSWYPFYAR LDNQGKFNAW
TAQSNSASEW LQIDLGSQRR VTGIITQGAR DFGHIQYVAA YKVAYSDDGV SWTEYRDQGA
LEGKIFPGNL DNNSHKKNMF ETPFLTRFVR ILPVAWHNRI TLRVELLGC
