ID A0A093RKW8_PYGAD Unreviewed; 1419 AA.
AC A0A093RKW8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:KFW71549.1};
DE Flags: Fragment;
GN ORFNames=AS28_11805 {ECO:0000313|EMBL:KFW71549.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW71549.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW71549.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW71549.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer; disulfide-linked.
CC {ECO:0000256|ARBA:ARBA00038769}.
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; KL225367; KFW71549.1; -; Genomic_DNA.
DR STRING; 9238.A0A093RKW8; -.
DR Proteomes; UP000054081; 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 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; 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; 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 PANTHER; PTHR11412:SF165; ALPHA-2-MACROGLOBULIN; 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; 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; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 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:UP000054081};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 422..570
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 692..782
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1324..1413
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW71549.1"
FT NON_TER 1419
FT /evidence="ECO:0000313|EMBL:KFW71549.1"
SQ SEQUENCE 1419 AA; 158087 MW; 8D8DA03E149280B9 CRC64;
YMVLLPFLIH TDSPEKVCVQ LTHLNESVTL SATLEYQGEN RSLIDDVVSE KDVFTCIPFS
LPKSNSQSPV TFLTVTVKGA TLQFRSRKSV LVKNSESLVF VQTDKPIYKP GQTVLFRIVS
LDKDFRPLNE VDPKKNRLYQ WAKAELKGGL IQLFFNLTSE PMQGTYTVVA QKVSGTTIRH
PFSVEEYVLP KFEVTVKMPK VITILDEKLK VTVCGLYTFG KPVPGLVSFR VCRKFEHADT
ACYGEEAKAV CDEFSGQTDN YGCISEMVKT KLFQLKRSGY ENKLHVEAKI KEEETGVELI
GTSFSEITTT ISKITFEHSD SHYKPGIPFF GQVKLVDGSG APIANEIVRI SLQGDQETNY
TTNEEGRARF ALNTSMLYFH SVGIRATHKV HPYCRDHSWV VPHYEGSYLQ LKRFYSPSNS
FLKIEPKSET LSCGSSTEVR VHYILTPEAI GEQKKIVFYY LVMAKGIIKQ AGTYILDLDQ
ESANGVFLLQ LPVQDDIAPV AQVLVYTTAP SREVIADSIK FSVEKCFSNK VDLSFSPSEG
LPSSDAHLLL RASPNSLCAV RAVDKSVLLM KPEADLSPSS VYSLLPMKEL HDYHHSPHVL
LEEPLENCVP LKKIVLNGIT YSPVVEVNEE DTYSILKEMG LKVFTNTKVR KPWYCSTENY
MPAGGRLPSA SIMSGMHGMR TSETVRKYFP ETWIWSLVSI SSEGNADLDV TIPDTITEWK
ANAFCTSADT GFGLSPTVSL RAFQPFFVEL TVPYSVVRGE AFMLKATVFN YLTTCIRVSV
TLAQSAHFLA APVKKEEESH CLCENGRKTV AWLVTPKSLG QVEFSVSTEA LQNQQPCGNT
IVETPEKGRK DTVIRQLLVE PEGVEKETTQ NSVLCVKGAP VKEKFSLLLP SNVVQDSGRA
YFSVLGDIMG TAMQNLHQLL QMPFGCGEQN MVLFAPNIYV LDYLNKTGQL SEEVKSKAIG
YLVSGYQRQL NYKHTDGSYS TFGPRYGQPG NTWLTAFVLK SFAQARPHIF IDEKHIQDAL
VWLSYKQKEN GCFHSSGTLL NNAMKGGVDN EVSLTAYITI ALLEIPLPVT HSVVRNGLFC
LETAADEKEN HVYTKALMAY AFALAGKEEK RKALLGSLEK EAVKKDGSVH WQRPGKEPEV
DLPYYRYRAP SAEVEMTAYV LLAHLTTQPA PSQEELSFAS LIAKWISSQQ NPSGGFSSTQ
DTVVALQALS LYGAVTYAKS GAASKVTLRS GGDFQQDFQV DPTNRLLLQR VPLPQVPGEY
STEVSGEGCV YLQTSLRYNV QPTQEDVPFM LHVYTIPETC EDSKAHKVFD IGINVSYTGE
RNGSNMVIVD VKMLSGFIPV KSSVRKLSTT WFHQIKRTEV STNHVLLYIE QLSSETLSFS
FTVERDIPVQ GLKPAQGKVY DYYETDEFAT QEYSAPCTA
//