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Protein

Lactadherin

Gene

Mfge8

Organism
Mus musculus (Mouse)
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. 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
Complete GO annotation...

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: MGI
  5. extrinsic component of plasma membrane Source: MGI
  6. membrane Source: MGI
  7. vesicle Source: MGI
Complete GO annotation...

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

BgeeiP21956.
CleanExiMM_MFGE8.
ExpressionAtlasiP21956. baseline and differential.
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 – 3165Combined sources
Beta strandi323 – 3275Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi359 – 3624Combined sources
Beta strandi367 – 38418Combined sources
Beta strandi393 – 40614Combined sources
Beta strandi414 – 4163Combined sources
Turni425 – 4273Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi438 – 45316Combined sources
Beta strandi455 – 4628Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000236278.
HOVERGENiHBG002385.
InParanoidiP21956.
KOiK17253.
OMAiFPGNLDN.
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

        10         20         30         40         50
MQVSRVLAAL CGMLLCASGL FAASGDFCDS SLCLNGGTCL TGQDNDIYCL
60 70 80 90 100
CPEGFTGLVC NETERGPCSP NPCYNDAKCL VTLDTQRGDI FTEYICQCPV
110 120 130 140 150
GYSGIHCETE TNYYNLDGEY MFTTAVPNTA VPTPAPTPDL SNNLASRCST
160 170 180 190 200
QLGMEGGAIA DSQISASSVY MGFMGLQRWG PELARLYRTG IVNAWTASNY
210 220 230 240 250
DSKPWIQVNL LRKMRVSGVM TQGASRAGRA EYLKTFKVAY SLDGRKFEFI
260 270 280 290 300
QDESGGDKEF LGNLDNNSLK VNMFNPTLEA QYIKLYPVSC HRGCTLRFEL
310 320 330 340 350
LGCELHGCSE PLGLKNNTIP DSQMSASSSY KTWNLRAFGW YPHLGRLDNQ
360 370 380 390 400
GKINAWTAQS NSAKEWLQVD LGTQRQVTGI ITQGARDFGH IQYVASYKVA
410 420 430 440 450
HSDDGVQWTV YEEQGSSKVF QGNLDNNSHK KNIFEKPFMA RYVRVLPVSW
460
HNRITLRLEL LGC
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP21956. 1 interaction.
MINTiMINT-4101815.

PTM databases

PhosphoSiteiP21956.

Proteomic databases

MaxQBiP21956.
PaxDbiP21956.
PRIDEiP21956.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi4240.
MGIiMGI:102768. Mfge8.

Phylogenomic databases

eggNOGiNOG151024.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000236278.
HOVERGENiHBG002385.
InParanoidiP21956.
KOiK17253.
OMAiFPGNLDN.
OrthoDBiEOG7ZWD1D.
TreeFamiTF330156.

Enzyme and pathway databases

ReactomeiREACT_198563. Amyloids.

Miscellaneous databases

ChiTaRSiMfge8. mouse.
NextBioi291842.
PROiP21956.
SOURCEiSearch...

Gene expression databases

BgeeiP21956.
CleanExiMM_MFGE8.
ExpressionAtlasiP21956. baseline and differential.
GenevestigatoriP21956.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 129 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

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 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.