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P21956

- MFGM_MOUSE

UniProt

P21956 - MFGM_MOUSE

Protein

Lactadherin

Gene

Mfge8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Contributes to phagocytic removal of apoptotic cells in many tissues. 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 similarity. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization.By similarity2 Publications

    GO - Molecular functioni

    1. integrin binding Source: BHF-UCL
    2. phosphatidylethanolamine binding Source: MGI
    3. phosphatidylserine binding Source: MGI

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. phagocytosis, engulfment Source: MGI
    4. phagocytosis, recognition Source: MGI
    5. positive regulation of apoptotic cell clearance Source: BHF-UCL
    6. positive regulation of phagocytosis Source: MGI
    7. single fertilization Source: UniProtKB-KW

    Keywords - Biological processi

    Angiogenesis, Cell adhesion, Fertilization

    Enzyme and pathway databases

    ReactomeiREACT_198563. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactadherin
    Alternative name(s):
    MFGM
    Milk fat globule-EGF factor 8
    Short name:
    MFG-E8
    SED1
    Sperm surface protein SP47
    Short name:
    MP47
    Gene namesi
    Name:Mfge8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:102768. Mfge8.

    Subcellular locationi

    Membrane 1 Publication; Peripheral membrane protein 1 Publication. Secreted 1 Publication

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. extracellular matrix Source: Ensembl
    3. extracellular space Source: MGI
    4. extracellular vesicular exosome Source: Ensembl
    5. extrinsic component of plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 463441LactadherinPRO_0000007653Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 39By similarity
    Disulfide bondi33 ↔ 49By similarity
    Disulfide bondi51 ↔ 60By similarity
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi68 ↔ 79By similarity
    Disulfide bondi73 ↔ 96By similarity
    Disulfide bondi98 ↔ 107By similarity
    Disulfide bondi148 ↔ 303By similarity
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi290 ↔ 294By similarity
    Disulfide bondi308 ↔ 4631 Publication
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Isoform 1 also exists in both an O-glycosylated and a non-O-glycosylated form.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP21956.
    PaxDbiP21956.
    PRIDEiP21956.

    PTM databases

    PhosphoSiteiP21956.

    Expressioni

    Tissue specificityi

    Mammary epithelial cell surfaces and spermatozoan. Isoform 2 is present in brain, heart, kidney and spleen and at low levels in lung, liver, small intestine and testis.2 Publications

    Developmental stagei

    Isoform 1 and isoform 2 are detectable in mammary tissue from non-pregnant animals, with isoform 2 being predominant. Levels of isoform 1 increase during gestation and lactation while levels of isoform 2 decrease.2 Publications

    Inductioni

    Isoform 1 is induced by insulin, prolactin and hydrocortisone in mammary epithelial cells. Expression of isoform 2 is repressed by the same treatment.1 Publication

    Gene expression databases

    ArrayExpressiP21956.
    BgeeiP21956.
    CleanExiMM_MFGE8.
    GenevestigatoriP21956.

    Interactioni

    Protein-protein interaction databases

    IntActiP21956. 1 interaction.
    MINTiMINT-4101815.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi312 – 3165
    Beta strandi323 – 3275
    Beta strandi346 – 3483
    Beta strandi350 – 3523
    Beta strandi355 – 3573
    Beta strandi359 – 3624
    Beta strandi367 – 38418
    Beta strandi393 – 40614
    Beta strandi414 – 4163
    Turni425 – 4273
    Beta strandi430 – 4323
    Beta strandi434 – 4363
    Beta strandi438 – 45316
    Beta strandi455 – 4628

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L9LNMR-A306-463[»]
    ProteinModelPortaliP21956.
    SMRiP21956. Positions 28-112, 145-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 6138EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini64 – 10845EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini148 – 303156F5/8 type C 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini308 – 463156F5/8 type C 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi87 – 893Cell attachment site

    Domaini

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

    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

    eggNOGiNOG151024.
    GeneTreeiENSGT00740000114988.
    HOGENOMiHOG000236278.
    HOVERGENiHBG002385.
    InParanoidiQ3U8S9.
    KOiK17253.
    OMAiVAWHNRI.
    OrthoDBiEOG7ZWD1D.
    TreeFamiTF330156.

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    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.
    PF12661. hEGF. 1 hit.
    [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. Align

    Isoform 1 (identifier: P21956-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MQVSRVLAAL CGMLLCASGL FAASGDFCDS SLCLNGGTCL TGQDNDIYCL    50
    CPEGFTGLVC NETERGPCSP NPCYNDAKCL VTLDTQRGDI FTEYICQCPV 100
    GYSGIHCETE TNYYNLDGEY MFTTAVPNTA VPTPAPTPDL SNNLASRCST 150
    QLGMEGGAIA DSQISASSVY MGFMGLQRWG PELARLYRTG IVNAWTASNY 200
    DSKPWIQVNL LRKMRVSGVM TQGASRAGRA EYLKTFKVAY SLDGRKFEFI 250
    QDESGGDKEF LGNLDNNSLK VNMFNPTLEA QYIKLYPVSC HRGCTLRFEL 300
    LGCELHGCSE PLGLKNNTIP DSQMSASSSY KTWNLRAFGW YPHLGRLDNQ 350
    GKINAWTAQS NSAKEWLQVD LGTQRQVTGI ITQGARDFGH IQYVASYKVA 400
    HSDDGVQWTV YEEQGSSKVF QGNLDNNSHK KNIFEKPFMA RYVRVLPVSW 450
    HNRITLRLEL LGC 463
    Length:463
    Mass (Da):51,241
    Last modified:July 27, 2011 - v3
    Checksum:i6E19CBB494B22878
    GO
    Isoform 2 (identifier: P21956-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         110-147: ETNYYNLDGEYMFTTAVPNTAVPTPAPTPDLSNNLASR → G

    Show »
    Length:426
    Mass (Da):47,169
    Checksum:i0882EDA89B95C445
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351N → D AA sequence (PubMed:2122462)Curated
    Sequence conflicti168 – 1681S → Y in AAA39534. (PubMed:2122462)Curated
    Sequence conflicti196 – 1961T → H in AAA39534. (PubMed:2122462)Curated
    Sequence conflicti284 – 2841K → R in AAA39534. (PubMed:2122462)Curated
    Sequence conflicti284 – 2841K → R in CAA72380. (PubMed:9546740)Curated
    Sequence conflicti284 – 2841K → R in BAA35180. (PubMed:9920772)Curated
    Sequence conflicti284 – 2841K → R in BAA76386. (PubMed:9920772)Curated
    Sequence conflicti284 – 2841K → R in BAC40794. (PubMed:16141072)Curated
    Sequence conflicti284 – 2841K → R in BAE42274. (PubMed:16141072)Curated
    Sequence conflicti284 – 2841K → R in AAH03892. (PubMed:15489334)Curated
    Sequence conflicti284 – 2841K → R in AAH03904. (PubMed:15489334)Curated
    Sequence conflicti309 – 3091S → L in AAA39534. (PubMed:2122462)Curated
    Sequence conflicti395 – 3951A → E in AAA39534. (PubMed:2122462)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei110 – 14738ETNYY…NLASR → G in isoform 2. 5 PublicationsVSP_009880Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38337 mRNA. Translation: AAA39534.1.
    Y11684 mRNA. Translation: CAA72380.2.
    AB021130 mRNA. Translation: BAA35180.1.
    AB025280 mRNA. Translation: BAA76386.1.
    AK089211 mRNA. Translation: BAC40794.1.
    AK152088 mRNA. Translation: BAE30938.1.
    AK171143 mRNA. Translation: BAE42274.1.
    BC003892 mRNA. Translation: AAH03892.1.
    BC003904 mRNA. Translation: AAH03904.1.
    CCDSiCCDS21379.1. [P21956-1]
    CCDS39989.1. [P21956-2]
    PIRiA36479.
    RefSeqiNP_032620.2. NM_008594.2. [P21956-1]
    UniGeneiMm.1451.

    Genome annotation databases

    EnsembliENSMUST00000032825; ENSMUSP00000032825; ENSMUSG00000030605. [P21956-1]
    ENSMUST00000107409; ENSMUSP00000103032; ENSMUSG00000030605. [P21956-2]
    GeneIDi17304.
    KEGGimmu:17304.
    UCSCiuc009hxz.1. mouse. [P21956-1]
    uc009hyb.1. mouse. [P21956-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38337 mRNA. Translation: AAA39534.1 .
    Y11684 mRNA. Translation: CAA72380.2 .
    AB021130 mRNA. Translation: BAA35180.1 .
    AB025280 mRNA. Translation: BAA76386.1 .
    AK089211 mRNA. Translation: BAC40794.1 .
    AK152088 mRNA. Translation: BAE30938.1 .
    AK171143 mRNA. Translation: BAE42274.1 .
    BC003892 mRNA. Translation: AAH03892.1 .
    BC003904 mRNA. Translation: AAH03904.1 .
    CCDSi CCDS21379.1. [P21956-1 ]
    CCDS39989.1. [P21956-2 ]
    PIRi A36479.
    RefSeqi NP_032620.2. NM_008594.2. [P21956-1 ]
    UniGenei Mm.1451.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L9L NMR - A 306-463 [» ]
    ProteinModelPortali P21956.
    SMRi P21956. Positions 28-112, 145-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21956. 1 interaction.
    MINTi MINT-4101815.

    PTM databases

    PhosphoSitei P21956.

    Proteomic databases

    MaxQBi P21956.
    PaxDbi P21956.
    PRIDEi P21956.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032825 ; ENSMUSP00000032825 ; ENSMUSG00000030605 . [P21956-1 ]
    ENSMUST00000107409 ; ENSMUSP00000103032 ; ENSMUSG00000030605 . [P21956-2 ]
    GeneIDi 17304.
    KEGGi mmu:17304.
    UCSCi uc009hxz.1. mouse. [P21956-1 ]
    uc009hyb.1. mouse. [P21956-2 ]

    Organism-specific databases

    CTDi 4240.
    MGIi MGI:102768. Mfge8.

    Phylogenomic databases

    eggNOGi NOG151024.
    GeneTreei ENSGT00740000114988.
    HOGENOMi HOG000236278.
    HOVERGENi HBG002385.
    InParanoidi Q3U8S9.
    KOi K17253.
    OMAi VAWHNRI.
    OrthoDBi EOG7ZWD1D.
    TreeFami TF330156.

    Enzyme and pathway databases

    Reactomei REACT_198563. Amyloids.

    Miscellaneous databases

    ChiTaRSi MFGE8. mouse.
    NextBioi 291842.
    PROi P21956.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21956.
    Bgeei P21956.
    CleanExi MM_MFGE8.
    Genevestigatori P21956.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR008979. Galactose-bd-like.
    IPR027060. Lactadherin.
    [Graphical view ]
    PANTHERi PTHR10127:SF303. PTHR10127:SF303. 1 hit.
    Pfami PF00008. EGF. 2 hits.
    PF00754. F5_F8_type_C. 2 hits.
    PF12661. hEGF. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 2 hits.
    SM00231. FA58C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    PROSITEi PS00022. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of a mouse mammary epithelial cell surface protein reveals the existence of epidermal growth factor-like domains linked to factor VIII-like sequences."
      Stubbs J.D., Lekutis C., Singer K.L., Bui A., Yuzuki D., Srinivasan U., Parry G.
      Proc. Natl. Acad. Sci. U.S.A. 87:8417-8421(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 23-35, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
      Strain: BALB/c.
      Tissue: Mammary gland.
    2. Ensslin M.A.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    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 23-463 (ISOFORM 2).
      Tissue: Testis.
    4. "Lactation-dependent expression of an mRNA splice variant with an exon for a multiply O-glycosylated domain of mouse milk fat globule glycoprotein MFG-E8."
      Oshima K., Aoki N., Negi M., Kishi M., Kitajima K., Matsuda T.
      Biochem. Biophys. Res. Commun. 254:522-528(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, GLYCOSYLATION.
      Strain: BALB/c.
      Tissue: Mammary gland.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow and Dendritic cell.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Mammary gland.
    7. Cited for: INTERACTION WITH ITGB3 AND ITGB5, FUNCTION IN NEOVASCULARIZATION.
    8. "Milk fat globule-EGF factor 8/lactadherin plays a crucial role in maintenance and repair of murine intestinal epithelium."
      Bu H.F., Zuo X.L., Wang X., Ensslin M.A., Koti V., Hsueh W., Raymond A.S., Shur B.D., Tan X.D.
      J. Clin. Invest. 117:3673-3683(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GUT EPITHELIAL REPAIR.
    9. "NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine."
      Ye H., Li B., Subramanian V., Choi B.H., Liang Y., Harikishore A., Chakraborty G., Baek K., Yoon H.S.
      Biochim. Biophys. Acta 1828:1083-1093(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 306-463, DISULFIDE BOND.

    Entry informationi

    Entry nameiMFGM_MOUSE
    AccessioniPrimary (citable) accession number: P21956
    Secondary accession number(s): P97800
    , Q3TBN5, Q3U8S9, Q9R1X9, Q9WTS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3