FETUA_RABIT
ID FETUA_RABIT Reviewed; 360 AA.
AC P80191; O18997;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Alpha-2-HS-glycoprotein;
DE AltName: Full=Fetuin-A;
DE AltName: Full=Haemonectin;
DE Flags: Precursor; Fragment;
GN Name=AHSG; Synonyms=FETUA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RA Osawa M., Saito T., Takeichi S.;
RT "Nucleotide sequence of cDNA encoding rabbit fetuin.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 19-26; 55-62; 118-128; 235-250 AND 332-344.
RC STRAIN=New Zealand white; TISSUE=Bone marrow;
RX PubMed=7682944; DOI=10.1111/j.1432-1033.1993.tb17790.x;
RA White H., Totty N., Panayotou G.;
RT "Haemonectin, a granulocytic-cell-binding protein, is related to the plasma
RT glycoprotein fetuin.";
RL Eur. J. Biochem. 213:523-528(1993).
CC -!- FUNCTION: A cell adhesion protein that binds immature cells of the
CC granulocyte lineage.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Bone marrow.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P02765}.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00861}.
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DR EMBL; D67014; BAA22653.1; -; mRNA.
DR PIR; S30340; S30340.
DR AlphaFoldDB; P80191; -.
DR SMR; P80191; -.
DR STRING; 9986.ENSOCUP00000001775; -.
DR MEROPS; I25.020; -.
DR PRIDE; P80191; -.
DR eggNOG; ENOG502RYRI; Eukaryota.
DR InParanoid; P80191; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006953; P:acute-phase response; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR CDD; cd00042; CY; 2.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR025760; Cystatin_Fetuin_A.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR001363; Prot_inh_fetuin_CS.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 2.
DR SUPFAM; SSF54403; SSF54403; 2.
DR PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
DR PROSITE; PS01254; FETUIN_1; 1.
DR PROSITE; PS01255; FETUIN_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL <1..15
FT /evidence="ECO:0000250"
FT CHAIN 16..360
FT /note="Alpha-2-HS-glycoprotein"
FT /id="PRO_0000008896"
FT DOMAIN 24..130
FT /note="Cystatin fetuin-A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DOMAIN 141..252
FT /note="Cystatin fetuin-A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT REGION 260..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29699"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02765"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 86..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 111..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 143..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 205..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT DISULFID 227..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT CONFLICT 126
FT /note="S -> P (in Ref. 1; BAA22653)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 360 AA; 38387 MW; F0908740610CBB95 CRC64;
LVLLLSLAQL WSCHLVTAVP LLGYREHNCD DPEAEQVALL AVDHINNHLQ QGYKHILNRI
DKVKVWPRRP TGEVYELEID TLETTCHALD PTPLANCSVR QVTQHAVEGD CDFHVLKQDG
QFTVLSAKCD STPDSAEDIL KLCPDCPLLT PLNDTRVAQA AEAALTAFNE KNNGAYLQLV
EIARAQLVPL PASTYVEFTV AATDCVAKEV TDPAKCNLLA DKQYGFCKAT VAEKVAREEV
EVTCTIFPAQ PVVPQPQPGV AGAAAVEPAP AVDPASPVSP PDGQSPSSLV VGPVLVAQAP
APPRAHYDLR QTFAGVPSME SGSGEAFHPG KVPVVVQPSV GAAPGPVITP CPGKVRYFKI
