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Q9D0F3

- LMAN1_MOUSE

UniProt

Q9D0F3 - LMAN1_MOUSE

Protein

Protein ERGIC-53

Gene

Lman1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961CarbohydratePROSITE-ProRule annotation
    Binding sitei129 – 1291CarbohydratePROSITE-ProRule annotation
    Metal bindingi160 – 1601CalciumPROSITE-ProRule annotation
    Metal bindingi162 – 1621Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi164 – 1641CalciumPROSITE-ProRule annotation
    Binding sitei164 – 1641CarbohydratePROSITE-ProRule annotation
    Binding sitei186 – 1861CarbohydratePROSITE-ProRule annotation
    Metal bindingi189 – 1891CalciumPROSITE-ProRule annotation
    Sitei508 – 5081Required for ER exportBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. endoplasmic reticulum organization Source: MGI
    2. ER to Golgi vesicle-mediated transport Source: MGI
    3. Golgi organization Source: Ensembl
    4. positive regulation of organelle organization Source: Ensembl
    5. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    Lectin, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_206143. Transport to the Golgi and subsequent modification.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein ERGIC-53
    Alternative name(s):
    ER-Golgi intermediate compartment 53 kDa protein
    Lectin mannose-binding 1
    p58
    Gene namesi
    Name:Lman1
    Synonyms:Ergic53
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1917611. Lman1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
    2. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. ER to Golgi transport vesicle Source: MGI
    5. Golgi apparatus Source: MGI
    6. Golgi membrane Source: UniProtKB-SubCell
    7. integral component of membrane Source: UniProtKB-KW
    8. sarcomere Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 517487Protein ERGIC-53PRO_0000017661Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi198 ↔ 238PROSITE-ProRule annotation
    Disulfide bondi473 – 473InterchainPROSITE-ProRule annotation
    Disulfide bondi482 – 482InterchainPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ9D0F3.
    PaxDbiQ9D0F3.
    PRIDEiQ9D0F3.

    PTM databases

    PhosphoSiteiQ9D0F3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D0F3.
    BgeeiQ9D0F3.
    CleanExiMM_LMAN1.
    GenevestigatoriQ9D0F3.

    Interactioni

    Subunit structurei

    Exists both as a covalent disulfide-linked homohexamer, and a complex of three disulfide-linked dimers non-covalently kept together. Interacts with MCFD2 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9D0F3. 6 interactions.
    MINTiMINT-1858436.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D0F3.
    SMRiQ9D0F3. Positions 43-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 484454LumenalSequence AnalysisAdd
    BLAST
    Topological domaini506 – 51712CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei485 – 50521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini52 – 275224L-type lectin-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni259 – 2613Carbohydrate bindingPROSITE-ProRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi516 – 5172ER export motifBy similarity

    Domaini

    The FF ER export motif at the C-terminus is not sufficient to support endoplasmic reticulum exit, and needs assistance of Gln-508 for proper recognition of COPII coat components.By similarity

    Sequence similaritiesi

    Contains 1 L-type lectin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292314.
    GeneTreeiENSGT00530000062977.
    HOVERGENiHBG052332.
    InParanoidiQ9D0F3.
    KOiK10080.
    OMAiGTVPFWA.
    OrthoDBiEOG7QC7VR.
    PhylomeDBiQ9D0F3.
    TreeFamiTF313311.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR005052. Lectin_leg.
    [Graphical view]
    PANTHERiPTHR12223. PTHR12223. 1 hit.
    PfamiPF03388. Lectin_leg-like. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9D0F3-1 [UniParc]FASTAAdd to Basket

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    MAVSRRRVPQ AGARSFFCAL LLSFSQFTGS DGTGGDAAAP GAAGTQAELP    50
    HRRFEYKYSF KGPHLVQSDG TVPFWAHAGN AIPSADQIRI APSLKSQRGS 100
    VWTKAKAAFE NWEVEVTFRV TGRGRIGADG LAIWYTENQG LDGPVFGSAD 150
    TWNGVGIFFD SFDNDGKKNN PAIVVIGNNG QINYDHQNDG ATQALASCQR 200
    DFRNKPYPVR AKITYYQKTL TVMINNGFTP DKNDYEFCAK VENMVIPTQG 250
    HFGISAATGG LADDHDVLSF LTFQLTEPGK EPPTAEKDIS EKEKEKYQEE 300
    FEHFQQELDK KKEEFQKGHP DLQGQPADDI FESIGDRELR QVFEGQNRIH 350
    LEIKQLNRQL DMILDEQRRY VSSLTEEISR RGAGTPGQPG QVSQQELDTV 400
    VKSQQEILRQ VNEVKNSMSE TVRLVSGIQH PGSAGVYETT QHFMDIKEHL 450
    HVVKRDIDSL AQRSMPSNEK PKCPDLPPFP SCLSTIHFVI FVVVQTVLFV 500
    GYIMYRTQQE AAAKKFF 517
    Length:517
    Mass (Da):57,789
    Last modified:June 1, 2001 - v1
    Checksum:iBA9FCFDEBCC5656D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011495 mRNA. Translation: BAB27655.1.
    BC057165 mRNA. Translation: AAH57165.1.
    CCDSiCCDS29313.1.
    RefSeqiNP_001165533.1. NM_001172062.1.
    NP_081676.1. NM_027400.3.
    UniGeneiMm.290857.
    Mm.449042.

    Genome annotation databases

    EnsembliENSMUST00000048260; ENSMUSP00000040140; ENSMUSG00000041891.
    ENSMUST00000120461; ENSMUSP00000113326; ENSMUSG00000041891.
    GeneIDi70361.
    KEGGimmu:70361.
    UCSCiuc008ffn.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011495 mRNA. Translation: BAB27655.1 .
    BC057165 mRNA. Translation: AAH57165.1 .
    CCDSi CCDS29313.1.
    RefSeqi NP_001165533.1. NM_001172062.1.
    NP_081676.1. NM_027400.3.
    UniGenei Mm.290857.
    Mm.449042.

    3D structure databases

    ProteinModelPortali Q9D0F3.
    SMRi Q9D0F3. Positions 43-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D0F3. 6 interactions.
    MINTi MINT-1858436.

    PTM databases

    PhosphoSitei Q9D0F3.

    Proteomic databases

    MaxQBi Q9D0F3.
    PaxDbi Q9D0F3.
    PRIDEi Q9D0F3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000048260 ; ENSMUSP00000040140 ; ENSMUSG00000041891 .
    ENSMUST00000120461 ; ENSMUSP00000113326 ; ENSMUSG00000041891 .
    GeneIDi 70361.
    KEGGi mmu:70361.
    UCSCi uc008ffn.2. mouse.

    Organism-specific databases

    CTDi 3998.
    MGIi MGI:1917611. Lman1.

    Phylogenomic databases

    eggNOGi NOG292314.
    GeneTreei ENSGT00530000062977.
    HOVERGENi HBG052332.
    InParanoidi Q9D0F3.
    KOi K10080.
    OMAi GTVPFWA.
    OrthoDBi EOG7QC7VR.
    PhylomeDBi Q9D0F3.
    TreeFami TF313311.

    Enzyme and pathway databases

    Reactomei REACT_206143. Transport to the Golgi and subsequent modification.

    Miscellaneous databases

    NextBioi 331450.
    PROi Q9D0F3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D0F3.
    Bgeei Q9D0F3.
    CleanExi MM_LMAN1.
    Genevestigatori Q9D0F3.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR005052. Lectin_leg.
    [Graphical view ]
    PANTHERi PTHR12223. PTHR12223. 1 hit.
    Pfami PF03388. Lectin_leg-like. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51328. L_LECTIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6J.
      Tissue: Embryo.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiLMAN1_MOUSE
    AccessioniPrimary (citable) accession number: Q9D0F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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