A1BG_RAT
ID A1BG_RAT Reviewed; 513 AA.
AC Q9EPH1; Q5EBD6; Q9JKL2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Alpha-1B-glycoprotein;
DE AltName: Full=Alpha-1-B glycoprotein;
DE AltName: Full=C44;
DE AltName: Full=Liver regeneration-related protein 1;
DE Flags: Precursor;
GN Name=A1bg {ECO:0000312|RGD:69417};
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] {ECO:0000305, ECO:0000312|EMBL:CAC19029.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAC19029.1};
RC TISSUE=Liver {ECO:0000312|EMBL:CAC19029.1};
RX PubMed=11356721; DOI=10.1210/endo.142.6.8193;
RA Gardmo C., Persson B., Mode A.;
RT "Cloning of a novel growth hormone-regulated rat complementary
RT deoxyribonucleic acid with homology to the human alpha1B-glycoprotein,
RT characterizing a new protein family.";
RL Endocrinology 142:2695-2701(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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] {ECO:0000305, ECO:0000312|EMBL:AAF68963.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 219-513 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000269|PubMed:11097837};
RC TISSUE=Liver {ECO:0000312|EMBL:AAF68963.1};
RX PubMed=11097837; DOI=10.1006/bbrc.2000.3792;
RA Xu W., Wang S., Wang G., Wei H., He F., Yang X.;
RT "Identification and characterization of differentially expressed genes in
RT the early response phase during liver regeneration.";
RL Biochem. Biophys. Res. Commun. 278:318-325(2000).
CC -!- SUBUNIT: Interacts with CRISP3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11356721};
CC IsoId=Q9EPH1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11097837};
CC IsoId=Q9EPH1-2; Sequence=VSP_051640, VSP_051641;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in normal liver. Isoform 2
CC is expressed in the regenerating liver after partial hepatectomy and at
CC very low levels in the normal lung, brain and testis.
CC {ECO:0000269|PubMed:11097837, ECO:0000269|PubMed:11356721}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Expressed in females at day 35 with
CC higher levels detected at day 56. Not detected in males of any age.
CC {ECO:0000269|PubMed:11356721}.
CC -!- INDUCTION: [Isoform 1]: Up-regulated by continuous exposure to growth
CC hormone. {ECO:0000269|PubMed:11356721}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ302031; CAC19029.1; -; mRNA.
DR EMBL; BC089771; AAH89771.1; -; mRNA.
DR EMBL; AF236054; AAF68963.1; ALT_INIT; mRNA.
DR RefSeq; NP_071594.2; NM_022258.2. [Q9EPH1-1]
DR AlphaFoldDB; Q9EPH1; -.
DR SMR; Q9EPH1; -.
DR STRING; 10116.ENSRNOP00000006273; -.
DR MEROPS; I43.950; -.
DR GlyGen; Q9EPH1; 7 sites.
DR SwissPalm; Q9EPH1; -.
DR PaxDb; Q9EPH1; -.
DR PRIDE; Q9EPH1; -.
DR Ensembl; ENSRNOT00000006273; ENSRNOP00000006273; ENSRNOG00000004692. [Q9EPH1-1]
DR GeneID; 140656; -.
DR KEGG; rno:140656; -.
DR UCSC; RGD:69417; rat. [Q9EPH1-1]
DR CTD; 1; -.
DR RGD; 69417; A1bg.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01050000244944; -.
DR HOGENOM; CLU_042929_1_0_1; -.
DR InParanoid; Q9EPH1; -.
DR OrthoDB; 1327293at2759; -.
DR PhylomeDB; Q9EPH1; -.
DR TreeFam; TF336644; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9EPH1; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004692; Expressed in liver and 4 other tissues.
DR Genevisible; Q9EPH1; RN.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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 Pfam; PF13895; Ig_2; 1.
DR PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..513
FT /note="Alpha-1B-glycoprotein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014503"
FT DOMAIN 22..126
FT /note="Ig-like V-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 127..219
FT /note="Ig-like V-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 220..312
FT /note="Ig-like V-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 313..415
FT /note="Ig-like V-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 416..513
FT /note="Ig-like V-type 5"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
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 153..195
FT /evidence="ECO:0000250|UniProtKB:P04217,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 245..292
FT /evidence="ECO:0000250|UniProtKB:P04217,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..392
FT /evidence="ECO:0000250|UniProtKB:P04217,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 441..488
FT /evidence="ECO:0000250|UniProtKB:P04217,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 417..473
FT /note="PAPKPRLEALWKGKVPLGHEAIFQCHGHVPRVSMELVREGFKTPFWMASTTS
FT TSAFL -> ELRRTMTEEGTERYSLRNQGSCAVISQLYLNEVLGFENLEEISLRCETWK
FT SGLFRIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11097837"
FT /id="VSP_051640"
FT VAR_SEQ 474..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11097837"
FT /id="VSP_051641"
FT CONFLICT 24
FT /note="D -> N (in Ref. 1; CAC19029)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="K -> E (in Ref. 1; CAC19029)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="T -> A (in Ref. 3; AAF68963)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="T -> M (in Ref. 3; AAF68963)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> K (in Ref. 3; AAF68963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56479 MW; 9CFA96A8BBC2ED1D CRC64;
MSLLTTVLLL WGFTLGPGNA LWLDSGSEPE LRAEPQSLLE PWANLTLVCA VDLPTKVFEL
IMNGWFLSQV RLETPVLSYR FSLGAITSNN SGVYRCRCGV EPPVDIQLPA LSKWTMLSNA
LEVTGKEPLP PPSAHADPVS WITPGGLPVY IMCRVAMRGV TYLLRKEGVD GTQKPDVQHK
GTAGFLIYKP GNYSCSYLTH AGGKPSEPSA IVTIKMSATQ LPPSLCLMGS YLTIYPQKTH
ETLACKAPRN AAEFQLRQGE RVLNIQGFSP TRDATIYYVN LKELDNQSPF TCRYRMHKYM
HVWSEDSKPV ELMWSDEKLP APVLTAEPSS HNLEPGSTVQ LRCTAHKAGL RFGLQRQGKP
DLVVVQMLNS SGTEAVFELH NISTIDSGNY SCIYMEQAPP FSGSASSEPL ELRINGPAPK
PRLEALWKGK VPLGHEAIFQ CHGHVPRVSM ELVREGFKTP FWMASTTSTS AFLKLSFVGP
QHTGNYSCRY TALSPFTFES GISDPVEVVV EGS
