FETUB_MOUSE
ID FETUB_MOUSE Reviewed; 388 AA.
AC Q9QXC1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Fetuin-B;
DE AltName: Full=Fetuin-like protein IRL685;
DE Flags: Precursor;
GN Name=Fetub;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=10947975; DOI=10.1042/bj3500589;
RA Olivier E., Soury E., Ruminy P., Husson A., Parmentier F., Daveau M.,
RA Salier J.-P.;
RT "Fetuin-B, a second member of the fetuin family in mammals.";
RL Biochem. J. 350:589-597(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23562279; DOI=10.1016/j.devcel.2013.03.001;
RA Dietzel E., Wessling J., Floehr J., Schafer C., Ensslen S., Denecke B.,
RA Rosing B., Neulen J., Veitinger T., Spehr M., Tropartz T., Tolba R.,
RA Renne T., Egert A., Schorle H., Gottenbusch Y., Hildebrand A.,
RA Yiallouros I., Stocker W., Weiskirchen R., Jahnen-Dechent W.;
RT "Fetuin-B, a liver-derived plasma protein is essential for fertilization.";
RL Dev. Cell 25:106-112(2013).
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.
CC {ECO:0000269|PubMed:23562279}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23562279}.
CC -!- TISSUE SPECIFICITY: Liver, lung and tongue.
CC -!- DISRUPTION PHENOTYPE: Female infertility due to a block early in
CC fertilization. Oocytes undergo premature zona pellucida hardening.
CC {ECO:0000269|PubMed:23562279}.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00862}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ242927; CAB62541.1; -; mRNA.
DR EMBL; BC018341; AAH18341.1; -; mRNA.
DR CCDS; CCDS37300.1; -.
DR RefSeq; NP_001077373.1; NM_001083904.1.
DR RefSeq; NP_001077374.1; NM_001083905.1.
DR RefSeq; NP_067539.1; NM_021564.2.
DR PDB; 6HPV; X-ray; 2.30 A; A=19-388.
DR PDB; 6HT9; X-ray; 3.10 A; B/D=19-388.
DR PDB; 7AUW; X-ray; 2.80 A; B/D=1-388.
DR PDBsum; 6HPV; -.
DR PDBsum; 6HT9; -.
DR PDBsum; 7AUW; -.
DR AlphaFoldDB; Q9QXC1; -.
DR SMR; Q9QXC1; -.
DR BioGRID; 208524; 2.
DR STRING; 10090.ENSMUSP00000023587; -.
DR MEROPS; I25.067; -.
DR GlyGen; Q9QXC1; 4 sites.
DR iPTMnet; Q9QXC1; -.
DR PhosphoSitePlus; Q9QXC1; -.
DR CPTAC; non-CPTAC-3371; -.
DR CPTAC; non-CPTAC-3372; -.
DR MaxQB; Q9QXC1; -.
DR PaxDb; Q9QXC1; -.
DR PRIDE; Q9QXC1; -.
DR ProteomicsDB; 271743; -.
DR Antibodypedia; 33852; 291 antibodies from 28 providers.
DR DNASU; 59083; -.
DR Ensembl; ENSMUST00000023587; ENSMUSP00000023587; ENSMUSG00000022871.
DR Ensembl; ENSMUST00000167399; ENSMUSP00000128745; ENSMUSG00000022871.
DR Ensembl; ENSMUST00000170805; ENSMUSP00000128989; ENSMUSG00000022871.
DR Ensembl; ENSMUST00000231768; ENSMUSP00000156347; ENSMUSG00000022871.
DR Ensembl; ENSMUST00000232097; ENSMUSP00000155898; ENSMUSG00000022871.
DR GeneID; 59083; -.
DR KEGG; mmu:59083; -.
DR UCSC; uc007yss.1; mouse.
DR CTD; 26998; -.
DR MGI; MGI:1890221; Fetub.
DR VEuPathDB; HostDB:ENSMUSG00000022871; -.
DR eggNOG; ENOG502S28K; Eukaryota.
DR GeneTree; ENSGT00950000182930; -.
DR InParanoid; Q9QXC1; -.
DR OMA; HRGFCLG; -.
DR PhylomeDB; Q9QXC1; -.
DR TreeFam; TF333729; -.
DR BioGRID-ORCS; 59083; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fetub; mouse.
DR PRO; PR:Q9QXC1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9QXC1; protein.
DR Bgee; ENSMUSG00000022871; Expressed in olfactory epithelium and 71 other tissues.
DR ExpressionAtlas; Q9QXC1; baseline and differential.
DR Genevisible; Q9QXC1; MM.
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; IDA:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR CDD; cd00042; CY; 2.
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; 2.
DR SMART; SM00043; CY; 2.
DR SUPFAM; SSF54403; SSF54403; 2.
DR PROSITE; PS51530; CYSTATIN_FETUIN_B; 2.
DR PROSITE; PS01254; FETUIN_1; 1.
DR PROSITE; PS01255; FETUIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Fertilization; Glycoprotein;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..388
FT /note="Fetuin-B"
FT /id="PRO_0000008900"
FT DOMAIN 28..141
FT /note="Cystatin fetuin-B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DOMAIN 152..264
FT /note="Cystatin fetuin-B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT REGION 270..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM5"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 292
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q58D62"
FT CARBOHYD 295
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q58D62"
FT DISULFID 96..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 120..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 154..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 217..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 237..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:7AUW"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 61..77
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7AUW"
FT STRAND 83..97
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:6HPV"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 188..214
FT /evidence="ECO:0007829|PDB:6HPV"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:7AUW"
FT STRAND 231..242
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6HT9"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:7AUW"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:6HT9"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:7AUW"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:6HPV"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:6HPV"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6HPV"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:6HPV"
SQ SEQUENCE 388 AA; 42713 MW; 39CFAD76A9D8DC2B CRC64;
MGLLRLLVLC TLAACCMARS PPAPPLPQRP LSPLHPLGCN DSEVLAVAGF ALQNINRDQK
DGYMLSLNRV HDVREHYQED MGSLFYLTLD VLETDCHVLS RKAQKDCKPR MFYESVYGQC
KAMFHINKPR RVLYLPAYNC TLRPVSKRKT HTTCPDCPSP IDLSNPSALE AATESLAKFN
SKSPSKKYEL VKVTKAMNQW VSGPAYYVEY LIKEAPCTKS QASCSLQHSD SEPVGICQGS
TVQSSLRHVP LIQPVEKSVT VTCEFFESQA QVPGDENPAV TQGPQKLPQK NTAPTSSPSV
TAPRGSIQHL PELDDEKPEE SKGGSPEEAF PVQLDLTTNP QGDTLDVSFL YLEPGDKKLV
VLPFPGKEQR SAECPGPEKE NNPLVLPP
