FETUB_RAT
ID FETUB_RAT Reviewed; 378 AA.
AC Q9QX79; F1LN83;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Fetuin-B;
DE AltName: Full=Fetuin-like protein IRL685;
DE Flags: Precursor;
GN Name=Fetub;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00862}.
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DR EMBL; AJ242926; CAB62543.1; -; mRNA.
DR EMBL; AABR06069363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_445800.2; NM_053348.2.
DR AlphaFoldDB; Q9QX79; -.
DR SMR; Q9QX79; -.
DR IntAct; Q9QX79; 3.
DR STRING; 10116.ENSRNOP00000051504; -.
DR MEROPS; I25.067; -.
DR GlyGen; Q9QX79; 4 sites.
DR iPTMnet; Q9QX79; -.
DR PhosphoSitePlus; Q9QX79; -.
DR SwissPalm; Q9QX79; -.
DR PaxDb; Q9QX79; -.
DR PRIDE; Q9QX79; -.
DR GeneID; 83928; -.
DR KEGG; rno:83928; -.
DR UCSC; RGD:69293; rat.
DR CTD; 26998; -.
DR RGD; 69293; Fetub.
DR eggNOG; ENOG502S28K; Eukaryota.
DR InParanoid; Q9QX79; -.
DR PRO; PR:Q9QX79; -.
DR Proteomes; UP000002494; Unplaced.
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; 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 2: Evidence at transcript 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..378
FT /note="Fetuin-B"
FT /id="PRO_0000008901"
FT DOMAIN 28..141
FT /note="Cystatin fetuin-B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DOMAIN 152..261
FT /note="Cystatin fetuin-B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT REGION 266..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 316
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:0000255"
FT CARBOHYD 289
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q58D62"
FT CARBOHYD 292
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..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT CONFLICT 88
FT /note="M -> T (in Ref. 1; CAB62543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 41563 MW; 7C49FF83E9FB30F5 CRC64;
MGVLRLLVLC TLAACCVARS PPAPPLPNAP FAPLRPLGCN DSEVLAVAGF ALQNINRVQK
DGYMLTLNRV HDARVHRQED MGSLFYLMLD VLETGCHVLS RKALKDCGPR IFYETVHGQC
KAMFHVNKPR RVLYLPAYNC TLRPVSKRKI HSMCPDCPHP VDLSAPSVLE AATESLAKFN
SENPSKQYAL VKVTKATTQW VVGPSYFVEY LIKESPCTQS QDSCSLQASD SEPVGLCQGS
LIKSPGVPPQ RFKKTVTVSC EFFESQDQVP GGENPADTQD AKKLPQKNTA PTSSPSITAP
RGSIQHLPEQ EEPEDSKGKS PEEPFPVQLD LTTNPQGDTL DVSFLYLEPE EKKLVVLPFP
GKEQRSPECP GPEKQRTP
