FETUB_BOVIN
ID FETUB_BOVIN Reviewed; 387 AA.
AC Q58D62;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Fetuin-B;
DE Flags: Precursor;
GN Name=FETUB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GLYCOSYLATION AT THR-292 AND THR-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA Darula Z., Medzihradszky K.F.;
RT "Affinity enrichment and characterization of mucin core-1 type
RT glycopeptides from bovine serum.";
RL Mol. Cell. Proteomics 8:2515-2526(2009).
CC -!- FUNCTION: Protease inhibitor required for egg fertilization. Required
CC to prevent premature zona pellucida hardening before fertilization,
CC probably by inhibiting the protease activity of ASTL, a protease that
CC mediates the cleavage of ZP2 and triggers zona pellucida hardening (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Liver and testis.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00862}.
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DR EMBL; BT021735; AAX46582.1; -; mRNA.
DR EMBL; BC103069; AAI03070.1; -; mRNA.
DR RefSeq; NP_001029390.1; NM_001034218.2.
DR AlphaFoldDB; Q58D62; -.
DR SMR; Q58D62; -.
DR STRING; 9913.ENSBTAP00000023309; -.
DR MEROPS; I25.066; -.
DR GlyConnect; 644; 1 N-Linked glycan (1 site), 2 O-Linked glycans (2 sites).
DR iPTMnet; Q58D62; -.
DR PaxDb; Q58D62; -.
DR PeptideAtlas; Q58D62; -.
DR PRIDE; Q58D62; -.
DR Ensembl; ENSBTAT00000023309; ENSBTAP00000023309; ENSBTAG00000017531.
DR GeneID; 504615; -.
DR KEGG; bta:504615; -.
DR CTD; 26998; -.
DR VEuPathDB; HostDB:ENSBTAG00000017531; -.
DR VGNC; VGNC:28955; FETUB.
DR eggNOG; ENOG502S28K; Eukaryota.
DR GeneTree; ENSGT00950000182930; -.
DR HOGENOM; CLU_044085_1_0_1; -.
DR InParanoid; Q58D62; -.
DR OMA; HRGFCLG; -.
DR OrthoDB; 1254847at2759; -.
DR TreeFam; TF333729; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000017531; Expressed in liver and 23 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR025764; Cystatin_Fetuin_B.
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; PS51530; CYSTATIN_FETUIN_B; 2.
DR PROSITE; PS01255; FETUIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Fertilization; Glycoprotein; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..387
FT /note="Fetuin-B"
FT /id="PRO_0000240346"
FT DOMAIN 25..139
FT /note="Cystatin fetuin-B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DOMAIN 150..258
FT /note="Cystatin fetuin-B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT REGION 264..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM5"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT CARBOHYD 295
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT DISULFID 94..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 118..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 152..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 217..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 238..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
SQ SEQUENCE 387 AA; 42663 MW; 271DB6FA333332E8 CRC64;
MNVLLLLVLC TLAMGCGATS PPQPAARPSS LLSLDCNSSY VLDIANDILQ DINRDRKDGY
VLSLNRVSDA REHRQEAGLG SLFYFTLDVL ETGCHVLSRT SWKNCEVRIF HESVYGQCKA
IFYINKEKRI FYLPAYNCTL RPVSQSAIIM TCPDCPSTSP YDLSNPRFME TATESLAKYN
SESPSKQYSL VKITKTSSQW VFGPAYFVEY LIKESPCVKS EGSSCALESP GSVPVGICHG
SLGEPQGNQG KIISVTCSFF NSQAPTPRGE NATVNQRPAN PSKTEELQQQ NTAPTNSPTK
AVPKGSVQYL PDWDKKREGS QEKDPVETFP VQLDLTTNPQ GESLDVSFLF QEPMEEKVVV
LPFPSKEQRS AECPGPAQKG YPFILPS
