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P01897

- HA1L_MOUSE

UniProt

P01897 - HA1L_MOUSE

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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

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
Complete GO annotation...

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_246972. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 309285ExtracellularSequence AnalysisAdd
BLAST
Transmembranei310 – 33122HelicalSequence AnalysisAdd
BLAST
Topological domaini332 – 36231CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

MaxQBiP01897.
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 – 3610Combined sources
Beta strandi39 – 424Combined sources
Beta strandi45 – 528Combined sources
Beta strandi55 – 617Combined sources
Beta strandi64 – 663Combined sources
Beta strandi70 – 734Combined sources
Turni74 – 763Combined sources
Helixi81 – 10828Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi131 – 14212Combined sources
Beta strandi145 – 1506Combined sources
Turni152 – 1554Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 17312Combined sources
Helixi176 – 18510Combined sources
Helixi187 – 19711Combined sources
Turni198 – 2003Combined sources
Helixi201 – 2044Combined sources
Beta strandi215 – 2173Combined sources
Turni219 – 2213Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi238 – 24710Combined sources
Turni249 – 2513Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi268 – 2736Combined sources
Turni275 – 2773Combined sources
Helixi278 – 2803Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi288 – 2903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4MS8X-ray1.92A25-203[»]
ProteinModelPortaliP01897.
SMRiP01897. Positions 25-292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01897.

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

        10         20         30         40         50
MGAMAPRTLL LLLAAALAPT QTRAGPHSMR YFETAVSRPG LGEPRYISVG
60 70 80 90 100
YVDNKEFVRF DSDAENPRYE PQAPWMEQEG PEYWERITQI AKGQEQWFRV
110 120 130 140 150
NLRTLLGYYN QSAGGTHTLQ WMYGCDVGSD GRLLRGYEQF AYDGCDYIAL
160 170 180 190 200
NEDLKTWTAA DMAAQITRRK WEQAGAAEYY RAYLEGECVE WLHRYLKNGN
210 220 230 240 250
ATLLRTDSPK AHVTHHPRSK GEVTLRCWAL GFYPADITLT WQLNGEELTQ
260 270 280 290 300
DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVYHEGL PEPLTLRWEP
310 320 330 340 350
PPSTDSYMVI VAVLGVLGAM AIIGAVVAFV MKRRRNTGGK GGDYALAPGS
360
QSSEMSLRDC KA
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4MS8 X-ray 1.92 A 25-203 [» ]
ProteinModelPortali P01897.
SMRi P01897. Positions 25-292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P01897. 2 interactions.
MINTi MINT-1535330.

Proteomic databases

MaxQBi P01897.
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.
REACT_246972. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

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: November 26, 2014
This is version 134 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