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MFGM_BOVIN
ID   MFGM_BOVIN              Reviewed;         427 AA.
AC   Q95114; P79344; Q27959;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Lactadherin;
DE   AltName: Full=BP47;
DE   AltName: Full=Components 15/16;
DE   AltName: Full=MFGM;
DE   AltName: Full=MGP57/53;
DE   AltName: Full=Milk fat globule-EGF factor 8;
DE            Short=MFG-E8;
DE   AltName: Full=PAS-6/PAS-7 glycoprotein;
DE   AltName: Full=SED1;
DE   AltName: Full=Sperm surface protein SP47;
DE   Flags: Precursor;
GN   Name=MFGE8;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT
RP   SER-27; THR-34; ASN-59 AND ASN-227.
RC   STRAIN=Holstein; TISSUE=Mammary gland;
RX   PubMed=8856064; DOI=10.1111/j.1432-1033.1996.0628h.x;
RA   Hvarregaard J., Andersen M.H., Berglund L., Rasmussen J.T., Petersen T.E.;
RT   "Characterization of glycoprotein PAS-6/7 from membranes of bovine milk fat
RT   globules.";
RL   Eur. J. Biochem. 240:628-636(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-427.
RC   TISSUE=Mammary gland;
RX   PubMed=8541316; DOI=10.1016/0304-4165(95)00110-7;
RA   Aoki N., Kishi M., Taniguchi Y., Adachi T., Nakamura R., Matsuda T.;
RT   "Molecular cloning of glycoprotein antigens MGP57/53 recognized by
RT   monoclonal antibodies raised against bovine milk fat globule membrane.";
RL   Biochim. Biophys. Acta 1245:385-391(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-427, AND TISSUE 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).
RN   [4]
RP   PROTEIN SEQUENCE OF 140-146; 174-187; 233-246 AND 422-427.
RC   TISSUE=Milk;
RX   PubMed=8485470;
RA   Mather I.H., Banghart L.R., Lane W.S.;
RT   "The major fat-globule membrane proteins, bovine components 15/16 and
RT   guinea-pig GP 55, are homologous to MGF-E8, a murine glycoprotein
RT   containing epidermal growth factor-like and factor V/VIII-like sequences.";
RL   Biochem. Mol. Biol. Int. 29:545-554(1993).
RN   [5]
RP   PROTEIN SEQUENCE OF 383-394.
RX   PubMed=1643094; DOI=10.1016/0167-4838(92)90325-8;
RA   Kim D.H., Kanno C., Mizokami Y.;
RT   "Purification and characterization of major glycoproteins, PAS-6 and PAS-7,
RT   from bovine milk fat globule membrane.";
RL   Biochim. Biophys. Acta 1122:203-211(1992).
RN   [6]
RP   FUNCTION.
RX   PubMed=10821695; DOI=10.1021/bi992221r;
RA   Andersen M.H., Graversen H., Fedosov S.N., Petersen T.E., Rasmussen J.T.;
RT   "Functional analyses of two cellular binding domains of bovine
RT   lactadherin.";
RL   Biochemistry 39:6200-6206(2000).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 270-427.
RX   PubMed=17583728; DOI=10.1016/j.jmb.2007.05.054;
RA   Lin L., Huai Q., Huang M., Furie B., Furie B.C.;
RT   "Crystal structure of the bovine lactadherin C2 domain, a membrane binding
RT   motif, shows similarity to the C2 domains of factor V and factor VIII.";
RL   J. Mol. Biol. 371:717-724(2007).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 270-427.
RX   PubMed=18160406; DOI=10.1074/jbc.m705195200;
RA   Shao C., Novakovic V.A., Head J.F., Seaton B.A., Gilbert G.E.;
RT   "Crystal structure of lactadherin C2 domain at 1.7A resolution with
RT   mutational and computational analyses of its membrane-binding motif.";
RL   J. Biol. Chem. 283:7230-7241(2008).
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:10821695}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q95114-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q95114-2; Sequence=VSP_001398;
CC   -!- TISSUE SPECIFICITY: Milk and spermatozoan. Also present in epididymis,
CC       kidney, heart, lymphatic gland and spleen but not esophagus, small
CC       intestine, muscle and liver. {ECO:0000269|PubMed:9546740}.
CC   -!- DOMAIN: The F5/8 type C 2 domain mediates high-affinity binding to
CC       phosphatidylserine-containing membranes. {ECO:0000250}.
CC   -!- PTM: The two O-linked glycans consist of Gal, GlcNAc and Fuc, with
CC       probably Fuc as reducing terminal sugar. {ECO:0000269|PubMed:8856064}.
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DR   EMBL; X91895; CAA62997.1; -; mRNA.
DR   EMBL; S80643; AAB35894.2; -; mRNA.
DR   EMBL; Y11719; CAA72406.1; -; mRNA.
DR   PIR; S74211; S74211.
DR   RefSeq; NP_788783.1; NM_176610.1.
DR   PDB; 2PQS; X-ray; 2.40 A; A/B/C/D=270-427.
DR   PDB; 3BN6; X-ray; 1.67 A; A=270-427.
DR   PDBsum; 2PQS; -.
DR   PDBsum; 3BN6; -.
DR   AlphaFoldDB; Q95114; -.
DR   SMR; Q95114; -.
DR   CORUM; Q95114; -.
DR   STRING; 9913.ENSBTAP00000004272; -.
DR   iPTMnet; Q95114; -.
DR   PaxDb; Q95114; -.
DR   PeptideAtlas; Q95114; -.
DR   PRIDE; Q95114; -.
DR   GeneID; 281913; -.
DR   KEGG; bta:281913; -.
DR   CTD; 4240; -.
DR   eggNOG; ENOG502RXUZ; Eukaryota.
DR   InParanoid; Q95114; -.
DR   EvolutionaryTrace; Q95114; -.
DR   Proteomes; UP000009136; 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   3D-structure; Alternative splicing; Angiogenesis; Cell adhesion;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Fertilization; Glycoprotein; Membrane; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT   CHAIN           19..427
FT                   /note="Lactadherin"
FT                   /id="PRO_0000007649"
FT   DOMAIN          20..59
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          62..106
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          109..265
FT                   /note="F5/8 type C 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          270..427
FT                   /note="F5/8 type C 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   MOTIF           85..87
FT                   /note="Cell attachment site"
FT   CARBOHYD        27
FT                   /note="O-linked (Fuc...) serine; in PAS-6"
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   CARBOHYD        34
FT                   /note="O-linked (Fuc...) threonine; in PAS-7"
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) (hybrid) asparagine; in PAS-6
FT                   and PAS-7"
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine; in
FT                   PAS-6"
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   DISULFID        24..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..47
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..265
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   DISULFID        252..256
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   DISULFID        270..427
FT                   /evidence="ECO:0000269|PubMed:8856064"
FT   VAR_SEQ         169..221
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001398"
FT   CONFLICT        19
FT                   /note="A -> F (in Ref. 1; CAA62997)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="L -> Q (in Ref. 1; CAA62997)"
FT                   /evidence="ECO:0000305"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          286..289
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   HELIX           298..300
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          313..315
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          329..345
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          352..369
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          388..391
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          394..417
FT                   /evidence="ECO:0007829|PDB:3BN6"
FT   STRAND          419..426
FT                   /evidence="ECO:0007829|PDB:3BN6"
SQ   SEQUENCE   427 AA;  47411 MW;  4CBBEE3A1DC4EB24 CRC64;
     MPCPRLLAAL FCSSGLFAAS GDFCDSSLCL HGGTCLLNED RTPPFYCLCP EGFTGLLCNE
     TEHGPCFPNP CHNDAECQVT DDSHRGDVFI QYICKCPLGY VGIHCETTCT SPLGMQTGAI
     ADSQISASSM HLGFMGLQRW APELARLHQT GIVNAWTSGN YDKNPWIQVN LMRKMWVTGV
     VTQGASRAGS AEYLKTFKVA YSTDGRQFQF IQVAGRSGDK IFIGNVNNSG LKINLFDTPL
     ETQYVRLVPI ICHRGCTLRF ELLGCELNGC TEPLGLKDNT IPNKQITASS YYKTWGLSAF
     SWFPYYARLD NQGKFNAWTA QTNSASEWLQ IDLGSQKRVT GIITQGARDF GHIQYVAAYR
     VAYGDDGVTW TEYKDPGASE SKIFPGNMDN NSHKKNIFET PFQARFVRIQ PVAWHNRITL
     RVELLGC
 
 
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