ID M3YHL1_MUSPF Unreviewed; 322 AA.
AC M3YHL1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Alpha-2-glycoprotein 1, zinc-binding {ECO:0000313|Ensembl:ENSMPUP00000010818.1};
DE SubName: Full=Zinc-alpha-2-glycoprotein {ECO:0000313|RefSeq:XP_004781894.1};
GN Name=AZGP1 {ECO:0000313|Ensembl:ENSMPUP00000010818.1,
GN ECO:0000313|RefSeq:XP_004781894.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010818.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010818.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004781894.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004781894.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MHC class I family.
CC {ECO:0000256|RuleBase:RU004439}.
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DR EMBL; AEYP01103970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01103971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004781894.1; XM_004781837.3.
DR STRING; 9669.ENSMPUP00000010818; -.
DR Ensembl; ENSMPUT00000010997.1; ENSMPUP00000010818.1; ENSMPUG00000010904.1.
DR GeneID; 101679584; -.
DR KEGG; mpuf:101679584; -.
DR CTD; 563; -.
DR eggNOG; ENOG502RWW3; Eukaryota.
DR GeneTree; ENSGT01100000263517; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR OMA; APYSCYV; -.
DR OrthoDB; 3840485at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl.
DR CDD; cd21010; IgC1_MHC-like_ZAG; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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 PANTHER; PTHR16675; MHC CLASS I-RELATED; 1.
DR PANTHER; PTHR16675:SF276; ZINC-ALPHA-2-GLYCOPROTEIN; 1.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..322
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118178"
FT DOMAIN 207..294
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 204..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 36408 MW; B316CE7DBB9BFA0A CRC64;
MDTIVSVLLS LLLLLGPAVP QETQAGPYSL SFFYTGLSRP RDGFPSFQAT AYLNDQDFFH
YDSEDRKAIP QYPWSQMEGL EDWEKESELQ KAREKIFMAT LTDIMDYYKD KEGSHTFQGM
FGCELRNDKN SGAFWRYAYD GRNFIEFNKE IPAWVPQDPA ALITKQKWEA EEVYVLRAKA
YLEEECPAML RRFLQHGKTY LDRQDPPSVS ITSHGTPGET QTLKCRADGF YPREIELHWI
HGGDTQETES GGDVLPSGNS TYQSWVVMSA SRQDGALDSY SCRVKHSSLA QPLTVLWPGA
RADGSEGSQG QEPPHLLAGE TS
//
