ID A0A091QE50_MERNU Unreviewed; 1738 AA.
AC A0A091QE50;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 8 {ECO:0000313|EMBL:KFQ23549.1};
DE Flags: Fragment;
GN ORFNames=N331_01333 {ECO:0000313|EMBL:KFQ23549.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ23549.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ23549.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ23549.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR EMBL; KK694619; KFQ23549.1; -; Genomic_DNA.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd02897; A2M_2; 1.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR022041; Methyltransf_FA.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412:SF139; C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 8; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF12248; Methyltransf_FA; 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 SMART; SM00280; KAZAL; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1692..1738
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ23549.1"
FT NON_TER 1738
FT /evidence="ECO:0000313|EMBL:KFQ23549.1"
SQ SEQUENCE 1738 AA; 193833 MW; 73CA9B13CDBAE7D5 CRC64;
GYLIAAPSVF RAGVEEAISV TIFNSVKETT VQIQLVVKGE TVSRGHGTIL DKGTIKLKVP
SGLRGQAHLK VWGNRHLAEE GYIFHNYTTV TIDSKGSSVF IQTDKPVYKP KQKVLINLFM
VTSDLRPVND RIEAYVVDPR GSRMIEWNNL KPFCCGIVNM TFPLSDQPVF GEWLIFAEMQ
GHTYNKSFEV QKYVLPKFEL LIEPPRYIRD LSLCEKGTVH ARYTFGKPVT GKLIVNMTIN
GVGYYRHEVG HPVLKTTQME GSAVFEVCVR DMMPADVPEH FRGTVSIWAT VISSDGSKQV
TFDDSTPVQK QLIDIKYSKD TRKQFKPGLP YKGKVEVTYP DGSPADRVTI RIKAELTPKD
NVYTSELVSR NGLVEFEIPS IPTAAQYVWL ETKVTAIDGK PSGDQYLPNY LSISSWYSPS
KCHIQLQAPD KPFQVGEEAW IAVKSTCPCN FTLHYEVASR GNIVLSGLQP SNITQQRSKR
ATLPFEKNSD ITHFPGTAPP SSPAAEVEVC VTFLHFSVVH TMAPLGRLLV FYVRENGEGV
TDSLQFTVQS SFENQVAVTL SANETRPGDV VNIKVRAAKS SCVCIATVDK SVYLLKPGFQ
LTASQVFQEL AEYDVSDAFG APKEEGHFWW PGMSSRRRRR SSVFPWHWDI TKDARFAFTE
TGLVVMTDIV SLNHRQNGGM YTDEAVPAFQ PHTGTLVATM HSKIAPSRAE KRKRTFFPET
WIWHCLNVSS FSGEAELHVE VPDSITTWIT EAVALSEEKG LGIASQTELK TFKPFFIDFT
LPYHVIRGEQ TKIPLTVYNY LALCVEVHVK ISVPKGIKFV GHPGKHHLTR KKCVAPGEAK
PTSIVLSFNE LGLSNITAKA FAYGGTNCCQ EGMQTLKSGK HTEDSYMDKR TPVGVDYVRS
SVIIEPEGLS REYTYSVFFC PNEKIHISTP NKYEYQYMQK PAQMTHFDIA VKAHNDAHLA
LSSGPHDMAE MTEIVIGGHQ NTKTWISISK MGEPVVSRDT AGILSWDEFR SFWISWKNGI
IQVGHGTRVL NESIIVEWTV PKQLEVKYIG FSTGWGSMGE FKIWRKEETD ENHNEAFTLG
VPHNIIPGSE RATASIIGDV MGPTLNNLDN LLRLPFGCGE QNMIHFAPNV FVLKYLQKTK
QLSREVESEA TDYLVQGYQR QLTYKRQDGS YSAFGERDSS GSMWLTAFVL KSFAQSRGFI
FIDPKELTAA KDWIIQHQKE DGSFPAMGRI LNKDIQGGIH GKISLTAYVV ASLLETGVTS
EEERTAVDKA KHFLESNLYS AEDPYSSALT AYALALLRSP AAAVPLRRMN SMALTQDGFT
HWSLTGTLVA DEDTFMGFND GLSQSVVSAE VEMTSYALLT YTLLGDVASA LPVVKWLSQQ
RNALGGFSST QDTCVALQAL AEYAILSYVG GVNLTISLAS TNLDYQETFE LNKMNKKVLQ
TAVIPSIPTG LFVSAKGEGC CLMQIDVTYN VPDPIAKPAF QLLVNLKEPK SEQHLQAPNL
LRSVSPDVSE ALHRERALGD DDDPASDQDH REYKVILETC TRWLHSGSSN MAVLEVPLFS
GFRADIESLE QLLMNKQIGL KRYEVDGRKV LFYFDEIPSQ CMTCVKFQAF REHIVGKTAP
VPIKVYDYYE PAFEATRFYN VSENSPLARE LCDGPTCNEV ESSASQWVGF VHSGPCNNVF
GCLEDEYFEQ CMCSRDCGYD GEPVCGSDGQ VYPNHCQMEV ASCRNNTRIE QMPMSQCS
//
