HA1F_CHICK
ID HA1F_CHICK Reviewed; 345 AA.
AC P15979;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Class I histocompatibility antigen, F10 alpha chain;
DE AltName: Full=B-F histocompatibility F10 antigen;
DE AltName: Full=B-F-beta-IV;
DE AltName: Full=B12;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B12; TISSUE=Liver;
RX PubMed=3141149; DOI=10.1002/j.1460-2075.1988.tb03132.x;
RA Guillemot F., Billault A., Pourquie O., Behar G., Chausse A.M., Zoorob R.,
RA Kreibich G., Auffray C.;
RT "A molecular map of the chicken major histocompatibility complex: the class
RT II beta genes are closely linked to the class I genes and the nucleolar
RT organizer.";
RL EMBO J. 7:2775-2785(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2370087; DOI=10.1007/bf02115020;
RA Kroemer G., Zoorob R., Auffray C.;
RT "Structure and expression of a chicken MHC class I gene.";
RL Immunogenetics 31:405-409(1990).
CC -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC immune system.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC microglobulin).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; X12780; CAA31272.1; -; mRNA.
DR EMBL; M31012; AAA48947.1; -; Genomic_DNA.
DR PIR; A45846; HLCHB4.
DR PDB; 5YMV; X-ray; 2.20 A; A/D=23-292.
DR PDB; 5YMW; X-ray; 2.00 A; A/D/G/J=23-292.
DR PDBsum; 5YMV; -.
DR PDBsum; 5YMW; -.
DR AlphaFoldDB; P15979; -.
DR SMR; P15979; -.
DR VEuPathDB; HostDB:geneid_693260; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..345
FT /note="Class I histocompatibility antigen, F10 alpha chain"
FT /id="PRO_0000018946"
FT TOPO_DOM 23..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..345
FT /note="Cytoplasmic"
FT DOMAIN 204..293
FT /note="Ig-like C1-type"
FT REGION 23..110
FT /note="Alpha-1"
FT REGION 111..201
FT /note="Alpha-2"
FT REGION 202..292
FT /note="Alpha-3"
FT REGION 293..301
FT /note="Connecting peptide"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 221..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 339
FT /note="P -> PDREGGSSSSST (in Ref. 2; AAA48947)"
FT /evidence="ECO:0000305"
FT STRAND 23..35
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5YMW"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 78..105
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:5YMW"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 216..229
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:5YMW"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:5YMW"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5YMW"
SQ SEQUENCE 345 AA; 38246 MW; 430DCCF8091B69A4 CRC64;
MGPCGALGLG LLLAAVCGAA APELHTLRYI QTAMTDPGPG QPWFVTVGYV DGELFVHYNS
TARRYVPRTE WIAAKADQQY WDGQTQIGQG NEQIDRENLG ILQRRYNQTG GSHTVQWMYG
CDILEGGPIR GYYQMAYDGR DFTAFDKGTM TFTAAVPEAV PTKRKWEEES EPERWKNYLE
ETCVEWLRRY VEYGKAELGR RERPEVRVWG KEADGILTLS CRAHGFYPRP IVVSWLKDGA
VRGQDAHSGG IVPNGDGTYH TWVTIDAQPG DGDKYQCRVE HASLPQPGLY SWEPPQPNLV
PIVAGVAVAI VAIAIMVGVG FIIYRRHAGK KGKGYNIAPG SNPAI
