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P05555

- ITAM_MOUSE

UniProt

P05555 - ITAM_MOUSE

Protein

Integrin alpha-M

Gene

Itgam

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Integrin alpha-M/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Alpha-M/beta-2 play a critical role in mast cell development and in immune complex-mediated glomerulonephritis. Mice expressing a null mutation of the alpha-M subunit gene demonstrate increase in neutrophil accumulation, in response to a impaired degranulation and phagocytosis, events that apparently accelerate apoptosis in neutrophils. These mice develop obesity.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi465 – 4739Sequence Analysis
    Calcium bindingi529 – 5379Sequence Analysis
    Calcium bindingi592 – 6009Sequence Analysis

    GO - Molecular functioni

    1. heparan sulfate proteoglycan binding Source: MGI
    2. heparin binding Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. opsonin binding Source: MGI

    GO - Biological processi

    1. activated T cell proliferation Source: MGI
    2. cell adhesion Source: MGI
    3. cellular extravasation Source: MGI
    4. integrin-mediated signaling pathway Source: UniProtKB-KW
    5. leukocyte cell-cell adhesion Source: MGI
    6. leukocyte migration involved in inflammatory response Source: MGI
    7. microglia development Source: MGI
    8. neutrophil chemotaxis Source: MGI
    9. single organismal cell-cell adhesion Source: MGI

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_216309. Integrin cell surface interactions.
    REACT_225233. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin alpha-M
    Alternative name(s):
    CD11 antigen-like family member B
    CR-3 alpha chain
    Cell surface glycoprotein MAC-1 subunit alpha
    Leukocyte adhesion receptor MO1
    CD_antigen: CD11b
    Gene namesi
    Name:Itgam
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:96607. Itgam.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. external side of plasma membrane Source: MGI
    3. integral component of membrane Source: MGI
    4. integrin complex Source: InterPro
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16161 PublicationAdd
    BLAST
    Chaini17 – 11531137Integrin alpha-MPRO_0000016290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi66 ↔ 73By similarity
    Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi105 ↔ 123By similarity
    Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi654 ↔ 711By similarity
    Glycosylationi696 – 6961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi770 ↔ 776By similarity
    Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi881 – 8811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi907 – 9071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi941 – 9411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi980 – 9801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi994 – 9941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi999 ↔ 1023By similarity
    Glycosylationi1022 – 10221N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1028 ↔ 1033By similarity
    Glycosylationi1045 – 10451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1051 – 10511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1076 – 10761N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP05555.
    PRIDEiP05555.

    PTM databases

    PhosphoSiteiP05555.

    Expressioni

    Tissue specificityi

    Predominantly expressed in monocytes and granulocytes.

    Gene expression databases

    ArrayExpressiP05555.
    BgeeiP05555.
    CleanExiMM_ITGAM.
    GenevestigatoriP05555.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain. Alpha-M associates with beta-2. Interacts with JAM3 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP05555. 2 interactions.
    MINTiMINT-4098963.

    Structurei

    3D structure databases

    ProteinModelPortaliP05555.
    SMRiP05555. Positions 17-146, 149-337, 344-1144.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 11051089ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1130 – 115324CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1106 – 112924HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati18 – 7558FG-GAP 1Add
    BLAST
    Repeati76 – 13560FG-GAP 2Add
    BLAST
    Domaini164 – 338175VWFAPROSITE-ProRule annotationAdd
    BLAST
    Repeati339 – 39052FG-GAP 3Add
    BLAST
    Repeati391 – 44454FG-GAP 4Add
    BLAST
    Repeati445 – 50359FG-GAP 5Add
    BLAST
    Repeati506 – 56459FG-GAP 6Add
    BLAST
    Repeati569 – 62961FG-GAP 7Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1132 – 11365GFFKR motif

    Domaini

    The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG301393.
    GeneTreeiENSGT00750000117471.
    HOGENOMiHOG000113114.
    HOVERGENiHBG100530.
    PhylomeDBiP05555.

    Family and domain databases

    InterProiIPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PRINTSiPR01185. INTEGRINA.
    SMARTiSM00191. Int_alpha. 5 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    PS50234. VWFA. 1 hit.
    [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: P05555-1) [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

    MTLKALLVTA LALCHGFNLD TEHPMTFQEN AKGFGQNVVQ LGGTSVVVAA     50
    PQEAKAVNQT GALYQCDYST SRCHPIPLQV PPEAVNMSLG LSLAVSTVPQ 100
    QLLACGPTVH QNCKENTYVN GLCYLFGSNL LRPPQQFPEA LRECPQQESD 150
    IVFLIDGSGS INNIDFQKMK EFVSTVMEQF KKSKTLFSLM QYSDEFRIHF 200
    TFNDFKRNPS PRSHVSPIKQ LNGRTKTASG IRKVVRELFH KTNGARENAA 250
    KILVVITDGE KFGDPLDYKD VIPEADRAGV IRYVIGVGNA FNKPQSRREL 300
    DTIASKPAGE HVFQVDNFEA LNTIQNQLQE KIFAIEGTQT GSTSSFEHEM 350
    SQEGFSASIT SNGPLLGSVG SFDWAGGAFL YTSKDKVTFI NTTRVDSDMN 400
    DAYLGYASAV ILRNRVQSLV LGAPRYQHIG LVVMFRENFG TWEPHTSIKG 450
    SQIGSYFGAS LCSVDMDADG NTNLILIGAP HYYEKTRGGQ VSVCPLPRGR 500
    ARWQCEALLH GDQGHPWGRF GAALTVLGDV NGDKLTDVAI GAPGEQENQG 550
    AVYIFYGASI ASLSASHSHR IIGAHFSPGL QYFGQSLSGG KDLTMDGLMD 600
    LAVGAQGHLL LLRAQPVLRL EATMEFSPKK VARSVFACQE QVLKNKDAGE 650
    VRVCLRVRKN TKDRLREGDI QSTVTYDLAL DPVRSRIRAF FDETKNNTRR 700
    RTQVFGLMQK CETLKLILPD CVDDSVSPII LRLNYTLVGE PLRSFGNLRP 750
    VLAMDAQRFF TAMFPFEKNC GNDSICQDDL SITMSAMGLD TLVVGGPQDF 800
    NMSVTLRNDG EDSYGTQVTV YYPSGLSYRK DSASQNPLTK KPWFVKPAES 850
    SSSSEGHGAL KSTTWNINHP IFPANSEVTF NVTFDVDSHA SFGNKLLLKA 900
    IVASENNMSR THKTKFQLEL PVKYAIYMIV TSDESSIRYL NFTASEMTSK 950
    VIQHQYQFNN LGQRSLPVSV VFWIPVQINN VTVWDHPQVI FSQNLSSACH 1000
    TEQKSPPHSN FRDQLERTPV LNCSVAVCKR IQCDLPSFNT QEIFNVTLKG 1050
    NLSFDWYIKT SHGHLLLVSS TEILFNDSAF ALLPGQESYV RSKTETKVEP 1100
    YEVHNPVPLI VGSSIGGLVL LALITAGLYK LGFFKRQYKD MMNEAAPQDA 1150
    PPQ 1153
    Length:1,153
    Mass (Da):127,481
    Last modified:February 1, 1991 - v2
    Checksum:i178DB988AECB0343
    GO
    Isoform 2 (identifier: P05555-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-569: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,036
    Mass (Da):115,196
    Checksum:i489843932CDBA7D2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371N → S in BAC30350. (PubMed:16141072)Curated
    Sequence conflicti683 – 6831V → G in BAC30350. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei453 – 569117Missing in isoform 2. 1 PublicationVSP_010473Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07640 mRNA. Translation: CAA30479.1.
    AK039444 mRNA. Translation: BAC30350.1.
    M14293 Genomic DNA. Translation: AAA39484.1.
    CCDSiCCDS21889.1. [P05555-1]
    PIRiS00551.
    UniGeneiMm.262106.

    Genome annotation databases

    EnsembliENSMUST00000106240; ENSMUSP00000101847; ENSMUSG00000030786.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07640 mRNA. Translation: CAA30479.1 .
    AK039444 mRNA. Translation: BAC30350.1 .
    M14293 Genomic DNA. Translation: AAA39484.1 .
    CCDSi CCDS21889.1. [P05555-1 ]
    PIRi S00551.
    UniGenei Mm.262106.

    3D structure databases

    ProteinModelPortali P05555.
    SMRi P05555. Positions 17-146, 149-337, 344-1144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P05555. 2 interactions.
    MINTi MINT-4098963.

    Chemistry

    BindingDBi P05555.
    ChEMBLi CHEMBL3603.

    PTM databases

    PhosphoSitei P05555.

    Proteomic databases

    PaxDbi P05555.
    PRIDEi P05555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000106240 ; ENSMUSP00000101847 ; ENSMUSG00000030786 .

    Organism-specific databases

    MGIi MGI:96607. Itgam.

    Phylogenomic databases

    eggNOGi NOG301393.
    GeneTreei ENSGT00750000117471.
    HOGENOMi HOG000113114.
    HOVERGENi HBG100530.
    PhylomeDBi P05555.

    Enzyme and pathway databases

    Reactomei REACT_216309. Integrin cell surface interactions.
    REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    ChiTaRSi ITGAM. mouse.
    PROi P05555.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05555.
    Bgeei P05555.
    CleanExi MM_ITGAM.
    Genevestigatori P05555.

    Family and domain databases

    InterProi IPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PRINTSi PR01185. INTEGRINA.
    SMARTi SM00191. Int_alpha. 5 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino acid sequence of the murine Mac-1 alpha chain reveals homology with the integrin family and an additional domain related to von Willebrand factor."
      Pytela R.
      EMBO J. 7:1371-1378(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Spinal cord.
    3. "A partial genomic DNA clone for the alpha subunit of the mouse complement receptor type 3 and cellular adhesion molecule Mac-1."
      Sastre L., Roman J.M., Teplow D.B., Dreyer W.J., Gee C.E., Larson R.S., Roberts T.M., Springer T.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:5644-5648(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-45.
      Strain: BALB/c.
      Tissue: Spleen.
    4. "Sequence homology of the LFA-1 and Mac-1 leukocyte adhesion glycoproteins and unexpected relation to leukocyte interferon."
      Springer T.A., Teplow D.B., Dreyer W.J.
      Nature 314:540-542(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-28.

    Entry informationi

    Entry nameiITAM_MOUSE
    AccessioniPrimary (citable) accession number: P05555
    Secondary accession number(s): Q8CA73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 136 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3