ID   A1BG_BOVIN              Reviewed;         503 AA.
AC   Q2KJF1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Alpha-1B-glycoprotein {ECO:0000250|UniProtKB:P04217};
DE   AltName: Full=Alpha-1-B glycoprotein {ECO:0000250|UniProtKB:P04217, ECO:0000312|EMBL:AAI05375.1};
DE   Flags: Precursor;
GN   Name=A1BG {ECO:0000312|EMBL:AAI05375.1};
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] {ECO:0000312|EMBL:AAI05375.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI05375.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:AAI05375.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 22-36, INTERACTION WITH CRISP3, AND GLYCOSYLATION.
RC   TISSUE=Serum {ECO:0000269|PubMed:20116414};
RX   PubMed=20116414; DOI=10.1016/j.bbagen.2010.01.011;
RA   Udby L., Johnsen A.H., Borregaard N.;
RT   "Human CRISP-3 binds serum alpha1B-glycoprotein across species.";
RL   Biochim. Biophys. Acta 1800:481-485(2010).
CC   -!- SUBUNIT: Interacts with CRISP3. {ECO:0000269|PubMed:20116414}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Plasma. {ECO:0000305}.
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DR   EMBL; BC105374; AAI05375.1; -; mRNA.
DR   RefSeq; NP_001039708.1; NM_001046243.2.
DR   AlphaFoldDB; Q2KJF1; -.
DR   SMR; Q2KJF1; -.
DR   STRING; 9913.ENSBTAP00000012837; -.
DR   MEROPS; I43.950; -.
DR   PaxDb; Q2KJF1; -.
DR   PeptideAtlas; Q2KJF1; -.
DR   PRIDE; Q2KJF1; -.
DR   Ensembl; ENSBTAT00000012837; ENSBTAP00000012837; ENSBTAG00000009735.
DR   GeneID; 518955; -.
DR   KEGG; bta:518955; -.
DR   CTD; 1; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009735; -.
DR   VGNC; VGNC:25433; A1BG.
DR   eggNOG; ENOG502RYEX; Eukaryota.
DR   GeneTree; ENSGT01050000244944; -.
DR   HOGENOM; CLU_042929_1_0_1; -.
DR   InParanoid; Q2KJF1; -.
DR   OrthoDB; 1327293at2759; -.
DR   TreeFam; TF336644; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000009735; Expressed in liver and 26 other tissues.
DR   ExpressionAtlas; Q2KJF1; baseline.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.10; -; 5.
DR   InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF13895; Ig_2; 1.
DR   PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; SSF48726; 5.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:20116414"
FT   CHAIN           22..503
FT                   /note="Alpha-1B-glycoprotein"
FT                   /evidence="ECO:0000269|PubMed:20116414"
FT                   /id="PRO_0000348606"
FT   DOMAIN          27..115
FT                   /note="Ig-like V-type 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..204
FT                   /note="Ig-like V-type 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          208..305
FT                   /note="Ig-like V-type 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          307..405
FT                   /note="Ig-like V-type 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          406..501
FT                   /note="Ig-like V-type 5"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..96
FT                   /evidence="ECO:0000250|UniProtKB:P04217,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        142..185
FT                   /evidence="ECO:0000250|UniProtKB:P04217,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        235..282
FT                   /evidence="ECO:0000250|UniProtKB:P04217,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        333..382
FT                   /evidence="ECO:0000250|UniProtKB:P04217,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        431..478
FT                   /evidence="ECO:0000250|UniProtKB:P04217,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   503 AA;  53554 MW;  22643DBA75DD4435 CRC64;
     MSAWAALLLL WGLSLSPVTE QATFFDPRPS LWAEAGSPLA PWADVTLTCQ SPLPTQEFQL
     LKDGVGQEPV HLESPAHEHR FPLGPVTSTT RGLYRCSYKG NNDWISPSNL VEVTGAEPLP
     APSISTSPVS WITPGLNTTL LCLSGLRGVT FLLRLEGEDQ FLEVAEAPEA TQATFPVHRA
     GNYSCSYRTH AAGTPSEPSA TVTIEELDPP PAPTLTVDRE SAKVLRPGSS ASLTCVAPLS
     GVDFQLRRGA EEQLVPRAST SPDRVFFRLS ALAAGDGSGY TCRYRLRSEL AAWSRDSAPA
     ELVLSDGTLP APELSAEPAI LSPTPGALVQ LRCRAPRAGV RFALVRKDAG GRQVQRVLSP
     AGPEAQFELR GVSAVDSGNY SCVYVDTSPP FAGSKPSATL ELRVDGPLPR PQLRALWTGA
     LTPGRDAVLR CEAEVPDVSF LLLRAGEEEP LAVAWSTHGP ADLVLTSVGP QHAGTYSCRY
     RTGGPRSLLS ELSDPVELRV AGS