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Protein

Lactadherin

Gene

MFGE8

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Cell adhesion, Fertilization

Names & Taxonomyi

Protein namesi
Recommended name:
Lactadherin
Alternative name(s):
BP47
Components 15/16
MFGM
MGP57/53
Milk fat globule-EGF factor 8
Short name:
MFG-E8
PAS-6/PAS-7 glycoprotein
SED1
Sperm surface protein SP47
Gene namesi
Name:MFGE8
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 427409LactadherinPRO_0000007649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 35By similarity
Glycosylationi27 – 271O-linked (Fuc...); in PAS-61 Publication
Disulfide bondi29 ↔ 47By similarity
Glycosylationi34 – 341O-linked (Fuc...); in PAS-71 Publication
Disulfide bondi49 ↔ 58By similarity
Glycosylationi59 – 591N-linked (GlcNAc...) (hybrid); in PAS-6 and PAS-71 Publication
Disulfide bondi66 ↔ 77By similarity
Disulfide bondi71 ↔ 94By similarity
Disulfide bondi96 ↔ 105By similarity
Disulfide bondi109 ↔ 2651 Publication
Glycosylationi227 – 2271N-linked (GlcNAc...) (high mannose); in PAS-61 Publication
Disulfide bondi252 ↔ 2561 Publication
Disulfide bondi270 ↔ 4271 Publication

Post-translational modificationi

The two O-linked glycans consist of Gal, GlcNAc and Fuc, with problably Fuc as reducing terminal sugar.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ95114.
PRIDEiQ95114.

Expressioni

Tissue specificityi

Milk and spermatozoan. Also present in epididymis, kidney, heart, lymphatic gland and spleen but not esophagus, small intestine, muscle and liver.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000004272.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi283 – 2853Combined sources
Beta strandi286 – 2894Combined sources
Helixi294 – 2963Combined sources
Helixi298 – 3003Combined sources
Helixi304 – 3063Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi329 – 34517Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi352 – 36918Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi394 – 41724Combined sources
Beta strandi419 – 4268Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PQSX-ray2.40A/B/C/D270-427[»]
3BN6X-ray1.67A270-427[»]
ProteinModelPortaliQ95114.
SMRiQ95114. Positions 270-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ95114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5940EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini62 – 10645EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 265157F5/8 type C 1PROSITE-ProRule annotationAdd
BLAST
Domaini270 – 427158F5/8 type C 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi85 – 873Cell attachment site

Domaini

The F5/8 type C 2 domain mediates high-affinity binding to phosphatidylserine-containing membranes.By similarity

Sequence similaritiesi

Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IFBC. Eukaryota.
ENOG41114BV. LUCA.
HOVERGENiHBG002385.
InParanoidiQ95114.
KOiK17253.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR027060. Lactadherin.
[Graphical view]
PANTHERiPTHR10127:SF303. PTHR10127:SF303. 1 hit.
PfamiPF00008. EGF. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q95114-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPCPRLLAAL FCSSGLFAAS GDFCDSSLCL HGGTCLLNED RTPPFYCLCP
60 70 80 90 100
EGFTGLLCNE TEHGPCFPNP CHNDAECQVT DDSHRGDVFI QYICKCPLGY
110 120 130 140 150
VGIHCETTCT SPLGMQTGAI ADSQISASSM HLGFMGLQRW APELARLHQT
160 170 180 190 200
GIVNAWTSGN YDKNPWIQVN LMRKMWVTGV VTQGASRAGS AEYLKTFKVA
210 220 230 240 250
YSTDGRQFQF IQVAGRSGDK IFIGNVNNSG LKINLFDTPL ETQYVRLVPI
260 270 280 290 300
ICHRGCTLRF ELLGCELNGC TEPLGLKDNT IPNKQITASS YYKTWGLSAF
310 320 330 340 350
SWFPYYARLD NQGKFNAWTA QTNSASEWLQ IDLGSQKRVT GIITQGARDF
360 370 380 390 400
GHIQYVAAYR VAYGDDGVTW TEYKDPGASE SKIFPGNMDN NSHKKNIFET
410 420
PFQARFVRIQ PVAWHNRITL RVELLGC
Length:427
Mass (Da):47,411
Last modified:November 1, 1997 - v2
Checksum:i4CBBEE3A1DC4EB24
GO
Isoform Short (identifier: Q95114-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-221: Missing.

Show »
Length:374
Mass (Da):41,573
Checksum:i093F675B73F26191
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191A → F in CAA62997 (PubMed:8856064).Curated
Sequence conflicti28 – 281L → Q in CAA62997 (PubMed:8856064).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 22153Missing in isoform Short. CuratedVSP_001398Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91895 mRNA. Translation: CAA62997.1.
S80643 mRNA. Translation: AAB35894.2.
Y11719 mRNA. Translation: CAA72406.1.
PIRiS74211.
RefSeqiNP_788783.1. NM_176610.1.
UniGeneiBt.5250.

Genome annotation databases

GeneIDi281913.
KEGGibta:281913.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91895 mRNA. Translation: CAA62997.1.
S80643 mRNA. Translation: AAB35894.2.
Y11719 mRNA. Translation: CAA72406.1.
PIRiS74211.
RefSeqiNP_788783.1. NM_176610.1.
UniGeneiBt.5250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PQSX-ray2.40A/B/C/D270-427[»]
3BN6X-ray1.67A270-427[»]
ProteinModelPortaliQ95114.
SMRiQ95114. Positions 270-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000004272.

Proteomic databases

PaxDbiQ95114.
PRIDEiQ95114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281913.
KEGGibta:281913.

Organism-specific databases

CTDi4240.

Phylogenomic databases

eggNOGiENOG410IFBC. Eukaryota.
ENOG41114BV. LUCA.
HOVERGENiHBG002385.
InParanoidiQ95114.
KOiK17253.

Miscellaneous databases

EvolutionaryTraceiQ95114.
NextBioi20805805.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR027060. Lactadherin.
[Graphical view]
PANTHERiPTHR10127:SF303. PTHR10127:SF303. 1 hit.
PfamiPF00008. EGF. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of glycoprotein PAS-6/7 from membranes of bovine milk fat globules."
    Hvarregaard J., Andersen M.H., Berglund L., Rasmussen J.T., Petersen T.E.
    Eur. J. Biochem. 240:628-636(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-27; THR-34; ASN-59 AND ASN-227.
    Strain: Holstein.
    Tissue: Mammary gland.
  2. "Molecular cloning of glycoprotein antigens MGP57/53 recognized by monoclonal antibodies raised against bovine milk fat globule membrane."
    Aoki N., Kishi M., Taniguchi Y., Adachi T., Nakamura R., Matsuda T.
    Biochim. Biophys. Acta 1245:385-391(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-427.
    Tissue: Mammary gland.
  3. "Molecular cloning and characterization of P47, a novel boar sperm-associated zona pellucida-binding protein homologous to a family of mammalian secretory proteins."
    Ensslin M.A., Vogel T., Calvete J.J., Thole H.H., Schmidtke J., Matsuda T., Toepfer-Petersen E.
    Biol. Reprod. 58:1057-1064(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-427, TISSUE SPECIFICITY.
    Tissue: Testis.
  4. "The major fat-globule membrane proteins, bovine components 15/16 and guinea-pig GP 55, are homologous to MGF-E8, a murine glycoprotein containing epidermal growth factor-like and factor V/VIII-like sequences."
    Mather I.H., Banghart L.R., Lane W.S.
    Biochem. Mol. Biol. Int. 29:545-554(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 140-146; 174-187; 233-246 AND 422-427.
    Tissue: Milk.
  5. "Purification and characterization of major glycoproteins, PAS-6 and PAS-7, from bovine milk fat globule membrane."
    Kim D.H., Kanno C., Mizokami Y.
    Biochim. Biophys. Acta 1122:203-211(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 383-394.
  6. "Functional analyses of two cellular binding domains of bovine lactadherin."
    Andersen M.H., Graversen H., Fedosov S.N., Petersen T.E., Rasmussen J.T.
    Biochemistry 39:6200-6206(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Crystal structure of the bovine lactadherin C2 domain, a membrane binding motif, shows similarity to the C2 domains of factor V and factor VIII."
    Lin L., Huai Q., Huang M., Furie B., Furie B.C.
    J. Mol. Biol. 371:717-724(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 270-427.
  8. "Crystal structure of lactadherin C2 domain at 1.7A resolution with mutational and computational analyses of its membrane-binding motif."
    Shao C., Novakovic V.A., Head J.F., Seaton B.A., Gilbert G.E.
    J. Biol. Chem. 283:7230-7241(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 270-427.

Entry informationi

Entry nameiMFGM_BOVIN
AccessioniPrimary (citable) accession number: Q95114
Secondary accession number(s): P79344, Q27959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 11, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.