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Database: UniProt
Entry: A0A452R4E5_URSAM
LinkDB: A0A452R4E5_URSAM
Original site: A0A452R4E5_URSAM 
ID   A0A452R4E5_URSAM        Unreviewed;      1468 AA.
AC   A0A452R4E5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Alpha-2-macroglobulin {ECO:0000313|Ensembl:ENSUAMP00000013288.1};
GN   Name=A2M {ECO:0000313|Ensembl:ENSUAMP00000013288.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000013288.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000013288.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   Ensembl; ENSUAMT00000014903.1; ENSUAMP00000013288.1; ENSUAMG00000009280.1.
DR   GeneTree; ENSGT00940000154904; -.
DR   Proteomes; UP000291022; 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   InterPro; IPR010916; TonB_box_CS.
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.
DR   PROSITE; PS00430; TONB_DEPENDENT_REC_1; 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:UP000291022};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1468
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019411444"
FT   DOMAIN          456..604
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          737..827
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1373..1460
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1468 AA;  163387 MW;  9A9BB41CFE40DE2E CRC64;
     MGKNKLFHPN LILLLLVFLP ADASVSGKPQ YMVLVPSLLH SETPEKGCLL LSYLNETVTV
     SASLESLREN RSLFTDLVVE KDLFHCVSFT VPRSPSNEEV MFLTIQVKGS TQEFKRRTTV
     VVKNQESLVF VQTDKPIYKP GQTVKFRIVS LDENFHPLNE LVSLQDPKGN RITQWQKLKL
     ENGLKQLSFA LSSEPFQGSY KVVVRKESGG ITEHAFTVEE FVLPKFEVQI TMPRIITILE
     EDVNVSVCGL YTYGKPVPGH MTMRVCRKYS NPSNCYSGES QAVCEKFSHQ LNSQGCFSQQ
     VKTKIFQMKR QGYEMKLEAE AKIQEEGTEV ELTGKGSTEI TRTITKLSFV KVDPYFRQGI
     PFFGQVQLLD GKGVPMPDEL VFITANEANY NSNATTDEHG LVQFSINTTD ITGTSLTVRV
     KHKDSSPCYG YQWLLAEHEE AHHTANLVFS LSKSFVRLEP LPRELPCGQT QTVQAHYILN
     ARVLQELNEL VFYYLIMAKG GVVLNGAHML PVKQGDMKGH FSVSIPVESD IAPVARMLIY
     AILPDGEVIG DSAKYKVENC LANKVDLSFR PTQSLPASHA HLQVSASPQS LCALRAVDQS
     VLLMKPEAEL SAASVYNLLP VKDLSGFPGS LNRQEEDDRD CINRHNVYIN GVMYSPVSNT
     NEKDMYSFLQ DMGLKVFTNT KIRKPKVCSQ PEHEAVYSSR RLFTSPAHLE LILRLQDSMV
     HVSEPLTETV RKYFPETWIW DLVAVDSSGV AEVGVIVPDT ITEWKAGALC LSNDTGLGLS
     LPASLRAFQP FFVELTMPYS VIRGEAFTLK ATVLNYLPKC IQVGVQLDPN PAFLVQEKEQ
     ESHCICGNGR HTVSWAVTPK ALGNVNFTVS AEALESQEPC GTEVAVVPEF GKKDTIIKSL
     LVEPEGLEKE VTFNSLLCPS GVEVSEQLPL KLPENVVEES ARASVSVLGD LLGSAMHNIQ
     NLLRMPYGCG EQNMVLFAPN IYVLNYLNET HQLTPEVMSK AVGYLNTGYQ RQLKYKHHDG
     SYSTFGENYG KSEGNTWLTA FVLKSFAQAR AYIFIDEAHI TQALTWLSQK QKDSGCFRSS
     GSLLNNAIKG GVEDEVTLSA YITIALLEIP LPATHPVVRN ALFCLESAWK SAKERPHGKH
     VYTKALLAYA FALAGNQDKR RETLDLLHGE AVKEDNSVHW ERPQKPRAPV GHFYQPPAPS
     AEVEMTSYVL LAYLTAQPAP TSEELTSAAR IVKWITKQQN SQGGFSSTQD TVVALQALSR
     YGTATFTRTG KPAQVTVQYS GTFVTKFQVD DDNRLLLQQT SLPKVPEEYT MTVTGEGCVY
     LQTSLKYNIL PEKAEFPFAL EVQTVPETCD GPKAHTSFQI SLNVSYIGSR PVSNMVIIDA
     KMVSGFIPLK PTVKMLERSN HVSRTEVSNN HVLIYLDKVT NQTLSLSFRV LQDVPVRELK
     PAIVKVYDYY ETDEFAIAEY SAPCSQGK
//
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