A1I3_RAT
ID A1I3_RAT Reviewed; 1477 AA.
AC P14046; Q4G042; Q63266; Q6LDP2; Q6LDR8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Alpha-1-inhibitor 3;
DE AltName: Full=Alpha-1-inhibitor 3 variant II;
DE Short=Alpha-1-inhibitor III;
DE Flags: Precursor;
GN Name=A1i3;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2831216; DOI=10.1016/s0021-9258(18)69025-8;
RA Braciak T.A., Northemann W., Hudson G.O., Shiels B.R., Gehring M.R.,
RA Fey G.H.;
RT "Sequence and acute phase regulation of rat alpha 1-inhibitor III messenger
RT RNA.";
RL J. Biol. Chem. 263:3999-4012(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
RC STRAIN=Fischer 344; TISSUE=Liver;
RX PubMed=2495816; DOI=10.1021/bi00427a013;
RA Northemann W., Shiels B.R., Braciak T.A., Fey G.H.;
RT "Structure and negative transcriptional regulation by glucocorticoids of
RT the acute-phase rat alpha 1-inhibitor III gene.";
RL Biochemistry 28:84-95(1989).
RN [3]
RP PROTEIN SEQUENCE OF 673-723.
RX PubMed=2472396; DOI=10.1016/s0021-9258(18)60482-x;
RA Enghild J.J., Salvesen G., Thogersen I.B., Pizzo S.V.;
RT "Proteinase binding and inhibition by the monomeric alpha-macroglobulin rat
RT alpha 1-inhibitor-3.";
RL J. Biol. Chem. 264:11428-11435(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 757-1477.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1253-1477.
RC TISSUE=Liver;
RX PubMed=2436907; DOI=10.1111/j.1432-1033.1987.tb11068.x;
RA Schweizer M., Takabayashi K., Geiger T., Laux T., Biermann G., Buhler J.M.,
RA Gauthier F., Roberts L.M., Heinrich P.C.;
RT "Identification and sequencing of cDNA clones for the rodent negative
RT acute-phase protein alpha 1-inhibitor 3.";
RL Eur. J. Biochem. 164:375-381(1987).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protease inhibitor with a wide spectrum of protein targets,
CC which attaches through its thioester function.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
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DR EMBL; J03552; AAA40628.1; -; mRNA.
DR EMBL; M22993; AAA79025.1; -; Genomic_DNA.
DR EMBL; BC098768; AAH98768.1; -; mRNA.
DR EMBL; M28297; AAA63493.1; -; mRNA.
DR EMBL; M28298; AAA63494.1; -; mRNA.
DR PIR; A29952; A29952.
DR AlphaFoldDB; P14046; -.
DR SMR; P14046; -.
DR IntAct; P14046; 1.
DR STRING; 10116.ENSRNOP00000040516; -.
DR MEROPS; I39.004; -.
DR GlyGen; P14046; 13 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P14046; -.
DR PhosphoSitePlus; P14046; -.
DR jPOST; P14046; -.
DR PaxDb; P14046; -.
DR PRIDE; P14046; -.
DR RGD; 1584999; LOC297568.
DR eggNOG; KOG1366; Eukaryota.
DR PhylomeDB; P14046; -.
DR PRO; PR:P14046; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Bait region; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..24
FT CHAIN 25..1477
FT /note="Alpha-1-inhibitor 3"
FT /id="PRO_0000000061"
FT REGION 601..750
FT /note="Bait region (approximate)"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..86
FT /evidence="ECO:0000250"
FT DISULFID 251..295
FT /evidence="ECO:0000250"
FT DISULFID 269..283
FT /evidence="ECO:0000250"
FT DISULFID 468..563
FT /evidence="ECO:0000250"
FT DISULFID 595..774
FT /evidence="ECO:0000250"
FT DISULFID 643..678
FT /evidence="ECO:0000250"
FT DISULFID 850..886
FT /evidence="ECO:0000250"
FT DISULFID 924..1324
FT /evidence="ECO:0000250"
FT DISULFID 1082..1130
FT /evidence="ECO:0000250"
FT DISULFID 1355..1470
FT /evidence="ECO:0000250"
FT CROSSLNK 975..978
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT CONFLICT 677
FT /note="Y -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1373
FT /note="M -> T (in Ref. 5; AAH98768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1406
FT /note="G -> E (in Ref. 5; AAA63494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1474
FT /note="D -> N (in Ref. 5; AAA63494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1477 AA; 163773 MW; 4DC05367C8385D2B CRC64;
MKKDREAQLC LFSALLAFLP FASLLNGNSK YMVLVPSQLY TETPEKICLH LYHLNETVTV
TASLISQRGT RKLFDELVVD KDLFHCVSFT IPRLPSSEEE ESLDINIEGA KHKFSERRVV
LVKNKESVVF VQTDKPMYKP GQSVKFRVVS MDKNLHPLNE LFPLAYIEDP KMNRIMQWQD
VKTENGLKQL SFSLSAEPIQ GPYKIVILKQ SGVKEEHSFT VMEFVLPRFG VDVKVPNAIS
VYDEIINVTA CATYTYGKPV PGHVKISLCH GNPTFSSETK SGCKEEDSRL DNNGCSTQEV
NITEFQLKEN YLKMHQAFHV NATVTEEGTG SEFSGSGRIE VERTRNKFLF LKADSHFRHG
IPFFVKVRLV DIKGDPIPNE QVLIKARDAG YTNATTTDQH GLAKFSIDTN GISDYSLNIK
VYHKEESSCI HSSCTAERHA EAHHTAYAVY SLSKSYIYLD TEAGVLPCNQ IHTVQAHFIL
KGQVLGVLQQ IVFHYLVMAQ GSILQTGNHT HQVEPGESQV QGNFALEIPV EFSMVPVAKM
LIYTILPDGE VIADSVKFQV EKCLRNKVHL SFSPSQSLPA SQTHMRVTAS PQSLCGLRAV
DQSVLLQKPE AELSPSLIYD LPGMQDSNFI ASSNDPFEDE DYCLMYQPIA REKDVYRYVR
ETGLMAFTNL KIKLPTYCNT DYDMVPLAVP AVALDSSTDR GMYESLPVVA VKSPLPQEPP
RKDPPPKDPV IETIRNYFPE TWIWDLVTVN SSGVTELEMT VPDTITEWKA GALCLSNDTG
LGLSSVASFQ AFQPFFVELT MPYSVIRGEA FTLKATVLNY LPTSLPMAVL LEASPDFTAV
PVENNQDSYC LGANGRHTSS WLVTPKSLGN VNFSVSAEAR QSPGPCGSEV ATVPETGRKD
TVVKVLIVEP EGIKKEHTFS SLLCASDAEL SETLSLLLPP TVVKDSARAH FSVMGDILSS
AIKNTQNLIQ MPYGCGEQNM VLFAPNIYVL KYLNETQQLT EKIKSKALGY LRAGYQRELN
YKHKDGSYSA FGDHNGQGQG NTWLTAFVLK SFAQARAFIF IDESHITDAF TWLSKQQKDS
GCFRSSGSLL NNAMKGGVDD EITLSAYITM ALLESSLPDT DPVVSKALSC LESSWENIEQ
GGNGSFVYTK ALMAYAFALA GNQEKRNEIL KSLDKEAIKE DNSIHWERPQ KPTKSEGYLY
TPQASSAEVE MSAYVVLARL TAQPAPSPED LALSMGTIKW LTKQQNSYGG FSSTQDTVVA
LDALSKYGAA TFSKSQKTPS VTVQSSGSFS QKFQVDKSNR LLLQQVSLPY IPGNYTVSVS
GEGCVYAQTT LRYNVPLEKQ QPAFALKVQT VPLTCNNPKG QNSFQISLEI SYMGSRPASN
MVIADVKMLS GFIPLKPTVK KLERLGHVSR TEVTTNNVLL YLDQVTNQTL SFSFIIQQDI
PVKNLQPAIV KVYDYYETDE VAFAEYSSPC SSDDQNV
