ID A0A3L8RYP2_CHLGU Unreviewed; 1868 AA.
AC A0A3L8RYP2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Kazal-like domain-containing protein {ECO:0000259|PROSITE:PS51465};
GN ORFNames=DV515_00014320 {ECO:0000313|EMBL:RLV90730.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV90730.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV90730.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV90730.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV90730.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV90730.1}.
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DR EMBL; QUSF01000119; RLV90730.1; -; Genomic_DNA.
DR Proteomes; UP000276834; 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:UP000276834};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1868
FT /note="Kazal-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018281861"
FT DOMAIN 1724..1771
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 1520..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1845..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1868 AA; 207720 MW; 9F28F651488EBE21 CRC64;
MAGCEPRRAR ALLLLLALCS LSAAQPRQRQ GYLIAAPSVF RSGVEEAISV TIFNSVKETT
VQIQLVVKGE TVSRSHGTVL DKGTIKLKVP SGLRGQAHLK VWGNRHLAEE GYIFHNYTTV
TIDSKGSSVF IQTDKPVYKP KQKVLINLFM VTSDLRPVND RIEAYVVDPR GSRMIEWNNL
KPFCCGIVNM TFPLSDQPVF GEWLIFAEMQ GHTYNKSFEV QKYVLPKFEL LIDPPRYIRD
LSLCEKGTVH ARYTFGKPVT GKLIVNMTIN GVGYYRHEVG HPVLKTMQID GSAAFEVCVR
DMMPADVPEH FRGTVNIWAT VISSDGSKQV TFDDSTPVQK QLIDIKYSKD TRKQFKPGLP
YKGKVEVTYP DGSPADRVTI RIKAELTPKD NVYTSELVSR NGLVEFEIPS IPTAAQYVWL
ETKVTAIDGK PSGDQYLPNY LSISSWYSPS KCHIQLQAPD KPFQVGEEAW IAVKSTCPCN
FTLHYEVASR GNIVLSGLQP SNVTQQRSKR ATTPFEKNID LTRFPETAPP SPPAAEVEVC
VTFLRFSVVH SMAPLARLLV YYVRENGEGV TDSLQFPVTS SFENQVAVTL SANETRPGDL
VNIKVRAAKG SCVCMATVDK SVYLLKTGFQ LTASQVFQEL AEYDVSDAFG APKEEGHFWW
PGMSSRRRRR SSVFPWHWDI TKDARFAFTE TGLVVMTDIV SLNHRQNGGM YTDEAVPAFQ
PHTGTLVATM HSKIAPSRAE KKKRTFFPET WIWHCLNVSG SSGEAQLQVE VPDSITTWIT
EAVALSEELG LGIARQTELK TFKPFFIDFT LPYHVIRGEQ TKIPLTVYNY LPLCAEVHVK
ISVPKGIKFV GHPGKHHLTR KKCVAPGEAK PTSIVLSFNE LGLSNITAKA FAYGGTNCCQ
EGMQSLKNGK HSEDSYMDKR SPVGVDYVRS SVIIEPEGLS REYTYSVFFC PNEKIHISTP
NKYEYQYMQK PAQMSHFDLA VKAHNDAHLA LSSGPHDMAE MTEIVIGGQQ NTRTWISTSK
MGEPVASRDT PGILSWDEFR SFWISWKNGI IQVGHGTRVL NESIIVEWTV PKQLEVKYIG
FSTGWGSMGE FKIWRKEETD ENHNEAFTLG VPHNIIPGSE RATASIIGDV MGPTLNNLDN
LLRLPFGCGE QNMIHFAPNV FVLKYLQKTK QLSHEVEVEA TDYLVQGYQR QLTYKRQDGS
YSAFGERDSS GSMWLTAFVL KSFAQSRGFI FIDPKELTAA KDWIIQHQKE DGSFPAMGRI
LNKDIQGGIH GKISLTAYVV ASLLETGVTS EEERTAVDKA KHFLECNLYS AEDPYTTALS
AYALSLLHSP SAAAVLRRMN SMAITQDGFT HWSLTGTLVT DEDTFMGFND GLSQSVVSAE
VEMTSYALLT YTLLGDVASA LPVVKWLSQQ RNALGGFSST QDTCVALQAL AEYAILSYVG
GVNLTISLAS TNLDYQETFE LNKMNKKVLQ TAVIPSIPTG LFVSAKGEGC CLMQIDVTYN
VPDPTAKAAF QLLVNLKEPK AEQHPPAPAP LRPGSAAERR AGALHRDRAL GDDEDPASDQ
DQREYKVILE TCTRWLHSGS SNMAVLEVPL FSGFRADIES LEQLLMNKQI GLKRYEVDGR
KVLFYFDEIP SQCMTCVKFQ AFREHIVGKT APVPIKVYDY YEPAFEATRF YNVSENSPLA
RELCDGPTCN EVESSASQWV GFVHSGPCNN IFGCLEDEYF EQCLCSRDCG YDGEPVCGSD
GHIYPNHCQM EVASCRNNTR IEQMPMSHCA ASKNLPEERE THSHTAEQPS VPQTPAAPAA
LVPPAAEEGP PLHTDLSYYS YEYDPDAFAV EGDVFEVVAE LSTASTFREG DSSQAEATPA
EWYTQTTL
//
