ID   A0A1S3W2D5_ERIEU        Unreviewed;      1459 AA.
AC   A0A1S3W2D5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=LOW QUALITY PROTEIN: alpha-2-macroglobulin-like {ECO:0000313|RefSeq:XP_016040550.1};
GN   Name=LOC103107053 {ECO:0000313|RefSeq:XP_016040550.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016040550.1};
RN   [1] {ECO:0000313|RefSeq:XP_016040550.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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   RefSeq; XP_016040550.1; XM_016185064.1.
DR   eggNOG; KOG1366; Eukaryota.
DR   InParanoid; A0A1S3W2D5; -.
DR   OrthoDB; 2970602at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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; MACROGLOBULIN / COMPLEMENT; 1.
DR   PANTHER; PTHR11412:SF133; MURINOGLOBULIN-1-RELATED; 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:UP000079721};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          458..606
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          723..813
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1359..1446
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1459 AA;  163867 MW;  3FA4A14097A53EA2 CRC64;
     MGKDRYTMSC LGVTYLALVS ATTLVLGNLQ YMVMVPYVLP TEIPVKICLL LRYLNETVTV
     SASLQHMERN LIDDLVIDKD LFHCISFTLP RSLSSKSERY LSVMIKGSTH EFHDAKKVLI
     QEKGSLIFIQ TDKQIYTPGQ SVKFRIVSMD EKFYPLHEVV SLSYMXDPEM NRIMQWQNVE
     LENGLTQLSF TVSSEPIKGS YKIVIMKQSG EKTEHSFTVE EYVLPKFEVQ VKVPKLINIL
     DTELNVSVCG IYSYRKPVSG NVTLRIEPIH MVPAYYFKNY AWPTYEEVNQ PLDIHGCITR
     QLNTNVFHLK TAEFKIEYLH VEAKITEEGT GLEIYGTGKT YVTKIITSLT FVKVDSYFRR
     GIPFTGQVRL VDRKGTPIPN ERIFIDSTAA NHHSNAITDE HGLAQFSIDT MNVMSSSLSV
     RVYHKHQSSC SWNRCWREEY QDAYRTVYHV FSLSNNAVKL EAVAGILPCN QIQTIQAHYI
     LNEQALGELK EMTFYYLIMA KGNIRKTGTY NLSMKAGESS GHFSMSFPVE AEFAPAVQLL
     IYAILPDGEV IGDKAKYEIE NCLSNKVDLS FNPTQSLPAS QALLQVTASP HSLCAVRAVD
     QSVLLKKPEA ELSATSIYNL LPKTDRSGLM NSLSKWQKDD KDCVKRDIVH NDDPNPTISR
     SEEQDIYIFI RDMNLVAFTN LKLKHPKFCS KALIMYSREK DYVVFANAPP SSIVTVRKYF
     PETWIWDLVT INSSGVAELR VTVPDTITEW KAGVFCLSNN TGFGISPTAS LRAFQPFFLE
     VTMPYSVIRG EAFTLKATVF NYVPKCIQVS VQLAPSPDYM AIPVEKEESH CLCTNGRLTV
     SWLVIPKSLG NVNFTVSAET VTSSELCGAE VATLPENGRR DTVVKLLLVE PEGIKKEHTF
     ISLLCASDDR LPEQLSLTLP PKIVEESTRA SFSVFGDILS SAIKNTQNLL QMPFGCGEQN
     MVLFAPNIYV LKYLNETQQV TEEIKSKAIG YLHAGYQRQL NYKHKDGSYS AFGDKDGKTQ
     GNTWLTAFVL KTLAQAQAVI FIDENHISEA LIWLSRKQTM SGCFSRSGTL LNNALKGGVQ
     DEVTLSAYIT IALLEIPLPV TNPVVQKALT CLESFWNKTK EKVDSHVYTK ALLAYAFALA
     GDQDKRREIL KSLDEDAIKE DNTMHWESPH KPRAPKNDFH TIQASSAEVE MTSYVLLAYL
     TTRSALTSED LTSATYIVKW LTKQQNPYGG FSSTQDTVVA LQALSRYGAA TFAKSEKDIL
     VTIQSSKTFS TKFQVNSTNR LLLQQVSLPD LPGEYSIQVS GEGCVYTQAV LKYNVFLEKK
     ESAFILQAQT VPQICDGPES HKSFQISLEV SYIGNRPVSN MVIVDVKMIS GFIPLKPTVK
     MLEKSSSVSR TEVTTNNVLI YLEQVTNQTL SFSFMVVQDI PVRDLKPAIV KVYDYYETDE
     VAFAEYNDPC STNSEQGNN
//