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P01897

- HA1L_MOUSE

UniProt

P01897 - HA1L_MOUSE

Protein

H-2 class I histocompatibility antigen, L-D alpha chain

Gene

H2-L

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Involved in the presentation of foreign antigens to the immune system.

    GO - Molecular functioni

    1. peptide antigen binding Source: InterPro

    GO - Biological processi

    1. antigen processing and presentation of peptide antigen via MHC class I Source: UniProtKB-KW
    2. defense response Source: MGI
    3. immune response Source: InterPro
    4. positive regulation of T cell mediated cytotoxicity Source: InterPro

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_197102. ER-Phagosome pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    H-2 class I histocompatibility antigen, L-D alpha chain
    Gene namesi
    Name:H2-L
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:95912. H2-L.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    2. MHC class I protein complex Source: UniProtKB-KW
    3. phagocytic vesicle membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, MHC I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 362338H-2 class I histocompatibility antigen, L-D alpha chainPRO_0000018932Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)
    Disulfide bondi125 ↔ 188
    Glycosylationi200 – 2001N-linked (GlcNAc...)
    Disulfide bondi227 ↔ 283
    Glycosylationi280 – 2801N-linked (GlcNAc...)Curated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP01897.

    Expressioni

    Gene expression databases

    GenevestigatoriP01897.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin).

    Protein-protein interaction databases

    IntActiP01897. 2 interactions.
    MINTiMINT-1535330.

    Structurei

    Secondary structure

    1
    362
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 3610
    Beta strandi39 – 424
    Beta strandi45 – 528
    Beta strandi55 – 617
    Beta strandi64 – 663
    Beta strandi70 – 734
    Turni74 – 763
    Helixi81 – 10828
    Beta strandi113 – 1153
    Beta strandi118 – 12710
    Beta strandi131 – 14212
    Beta strandi145 – 1506
    Turni152 – 1554
    Beta strandi157 – 1593
    Helixi162 – 17312
    Helixi176 – 18510
    Helixi187 – 19711
    Turni198 – 2003
    Helixi201 – 2044
    Beta strandi215 – 2173
    Turni219 – 2213
    Beta strandi223 – 2286
    Beta strandi231 – 2355
    Beta strandi238 – 24710
    Turni249 – 2513
    Beta strandi261 – 2633
    Beta strandi268 – 2736
    Turni275 – 2773
    Helixi278 – 2803
    Beta strandi282 – 2865
    Beta strandi288 – 2903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LD9X-ray2.40A/D25-292[»]
    1LDPX-ray3.10H25-296[»]
    2E7LX-ray2.50E/F25-205[»]
    2OI9X-ray2.35A25-203[»]
    3E2HX-ray3.80A25-199[»]
    3E3QX-ray2.95A/B/H/L/P/U/Y/c25-199[»]
    3ERYX-ray1.95A/B25-198[»]
    3TF7X-ray2.75A/E25-203[»]
    3TFKX-ray2.75A25-203[»]
    3TJHX-ray2.12A25-203[»]
    3TPUX-ray3.10E/I/K/Q25-203[»]
    3UO1X-ray1.64P70-78[»]
    3UYRX-ray1.70P70-77[»]
    3V4UX-ray1.64P70-78[»]
    3V52X-ray1.70P70-77[»]
    3VJ6X-ray1.90P3-11[»]
    ProteinModelPortaliP01897.
    SMRiP01897. Positions 25-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01897.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 309285ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini332 – 36231CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei310 – 33122HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini209 – 29789Ig-like C1-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 11490Alpha-1Add
    BLAST
    Regioni115 – 20692Alpha-2Add
    BLAST
    Regioni207 – 29892Alpha-3Add
    BLAST
    Regioni299 – 30911Connecting peptideAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MHC class I family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG016709.
    InParanoidiP01897.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR027648. MHC_I_a.
    IPR001039. MHC_I_a_a1/a2.
    IPR010579. MHC_I_a_C.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    PF06623. MHC_I_C. 1 hit.
    [Graphical view]
    PRINTSiPR01638. MHCCLASSI.
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01897-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LGEPRYISVG    50
    YVDNKEFVRF DSDAENPRYE PQAPWMEQEG PEYWERITQI AKGQEQWFRV 100
    NLRTLLGYYN QSAGGTHTLQ WMYGCDVGSD GRLLRGYEQF AYDGCDYIAL 150
    NEDLKTWTAA DMAAQITRRK WEQAGAAEYY RAYLEGECVE WLHRYLKNGN 200
    ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT WQLNGEELTQ 250
    DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP 300
    PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS 350
    QSSEMSLRDC KA 362
    Length:362
    Mass (Da):40,711
    Last modified:July 15, 1998 - v2
    Checksum:iA5EFDEE31177BF22
    GO

    Sequence cautioni

    The sequence CAA24126.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 248LAPTQTRA → WPDSDPR(PubMed:7058332)Curated
    Sequence conflicti17 – 248LAPTQTRA → WPDSDPR(PubMed:6604582)Curated
    Sequence conflicti17 – 248LAPTQTRA → WPDSDPR(PubMed:6952248)Curated
    Sequence conflicti35 – 351Missing(PubMed:7058332)Curated
    Sequence conflicti35 – 351Missing(PubMed:6604582)Curated
    Sequence conflicti145 – 1451C → R(PubMed:7058332)Curated
    Sequence conflicti145 – 1451C → R(PubMed:6604582)Curated
    Sequence conflicti145 – 1451C → R(PubMed:6952248)Curated
    Sequence conflicti220 – 2201K → E(PubMed:6895103)Curated
    Sequence conflicti292 – 2921E → H in CAA24129. (PubMed:6952248)Curated
    Sequence conflicti292 – 2921E → H in AAA39661. (PubMed:6952248)Curated
    Sequence conflicti303 – 3031S → F(PubMed:6895103)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33151 mRNA. Translation: AAA39659.1.
    V00749 Genomic DNA. Translation: CAA24126.1. Different initiation.
    V00750 Genomic DNA. Translation: CAA24127.1.
    V00751 Genomic DNA. Translation: CAA24128.1.
    V00752 Genomic DNA. Translation: CAA24129.1. Sequence problems.
    L00129 Genomic DNA. Translation: AAA39662.1.
    J00394 mRNA. Translation: AAA39578.1.
    L00128, L00127 Genomic DNA. Translation: AAA39661.1.
    PIRiB60854.
    C60854.
    I54069. HLMSLD.
    UniGeneiMm.439675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33151 mRNA. Translation: AAA39659.1 .
    V00749 Genomic DNA. Translation: CAA24126.1 . Different initiation.
    V00750 Genomic DNA. Translation: CAA24127.1 .
    V00751 Genomic DNA. Translation: CAA24128.1 .
    V00752 Genomic DNA. Translation: CAA24129.1 . Sequence problems.
    L00129 Genomic DNA. Translation: AAA39662.1 .
    J00394 mRNA. Translation: AAA39578.1 .
    L00128 , L00127 Genomic DNA. Translation: AAA39661.1 .
    PIRi B60854.
    C60854.
    I54069. HLMSLD.
    UniGenei Mm.439675.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LD9 X-ray 2.40 A/D 25-292 [» ]
    1LDP X-ray 3.10 H 25-296 [» ]
    2E7L X-ray 2.50 E/F 25-205 [» ]
    2OI9 X-ray 2.35 A 25-203 [» ]
    3E2H X-ray 3.80 A 25-199 [» ]
    3E3Q X-ray 2.95 A/B/H/L/P/U/Y/c 25-199 [» ]
    3ERY X-ray 1.95 A/B 25-198 [» ]
    3TF7 X-ray 2.75 A/E 25-203 [» ]
    3TFK X-ray 2.75 A 25-203 [» ]
    3TJH X-ray 2.12 A 25-203 [» ]
    3TPU X-ray 3.10 E/I/K/Q 25-203 [» ]
    3UO1 X-ray 1.64 P 70-78 [» ]
    3UYR X-ray 1.70 P 70-77 [» ]
    3V4U X-ray 1.64 P 70-78 [» ]
    3V52 X-ray 1.70 P 70-77 [» ]
    3VJ6 X-ray 1.90 P 3-11 [» ]
    ProteinModelPortali P01897.
    SMRi P01897. Positions 25-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P01897. 2 interactions.
    MINTi MINT-1535330.

    Proteomic databases

    PRIDEi P01897.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:95912. H2-L.

    Phylogenomic databases

    HOVERGENi HBG016709.
    InParanoidi P01897.

    Enzyme and pathway databases

    Reactomei REACT_197102. ER-Phagosome pathway.

    Miscellaneous databases

    EvolutionaryTracei P01897.
    PROi P01897.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P01897.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR027648. MHC_I_a.
    IPR001039. MHC_I_a_a1/a2.
    IPR010579. MHC_I_a_C.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    PF06623. MHC_I_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01638. MHCCLASSI.
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Generation of a functional cDNA encoding the LdH2 class-I molecule by using a single-LTR retroviral shuttle vector."
      Joly E., Oldstone M.B.
      Gene 97:213-221(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "DNA sequence of a gene encoding a BALB/c mouse Ld transplantation antigen."
      Moore K.W., Sher B.T., Sun Y.H., Eakle K.A., Hood L.E.
      Science 215:679-682(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (CLONE 27.5).
      Strain: BALB/c.
      Tissue: Sperm.
    3. "Expression and function of transplantation antigens with altered or deleted cytoplasmic domains."
      Zuniga M.C., Malissen B., McMillan M., Brayton P.R., Clark S.S., Forman J., Hood L.E.
      Cell 34:535-544(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BALB/c.
      Tissue: Sperm.
    4. "Structure and expression of a mouse major histocompatibility antigen gene, H-2Ld."
      Evans G.A., Margulies D.H., Camerini-Otero R.D., Ozato K., Seidman J.G.
      Proc. Natl. Acad. Sci. U.S.A. 79:1994-1998(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311 AND 339-348.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-362 (CLONE PH-2D-3).
    6. "The three-dimensional structure of an H-2Ld-peptide complex explains the unique interaction of Ld with beta-2 microglobulin and peptide."
      Balendiran G.K., Solheim J.C., Young A.C., Hansen T.H., Nathenson S.G., Sacchettini J.C.
      Proc. Natl. Acad. Sci. U.S.A. 94:6880-6885(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-293.

    Entry informationi

    Entry nameiHA1L_MOUSE
    AccessioniPrimary (citable) accession number: P01897
    Secondary accession number(s): Q31195, Q31196, Q31197
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 132 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, 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