ID V4CA32_LOTGI Unreviewed; 949 AA.
AC V4CA32;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LOTGIDRAFT_174075 {ECO:0000313|EMBL:ESO98654.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO98654.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO98654.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR EMBL; KB201224; ESO98654.1; -; Genomic_DNA.
DR RefSeq; XP_009050651.1; XM_009052403.1.
DR AlphaFoldDB; V4CA32; -.
DR STRING; 225164.V4CA32; -.
DR EnsemblMetazoa; LotgiT174075; LotgiP174075; LotgiG174075.
DR GeneID; 20242609; -.
DR KEGG; lgi:LOTGIDRAFT_174075; -.
DR CTD; 20242609; -.
DR HOGENOM; CLU_001634_3_0_1; -.
DR OMA; KRTINIC; -.
DR OrthoDB; 4033541at2759; -.
DR Proteomes; UP000030746; 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; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF171; PREGNANCY ZONE PROTEIN-LIKE PROTEIN; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 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 Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 25..115
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 659..753
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 949 AA; 106893 MW; B1C8E1B761E6D454 CRC64;
MAENNVVPGP TASKTLNLRT HFPETWLWQL DTVGETGKLQ KITEAPHTVT KWQGNTLCTN
PDVGFGLSPV ASLITFQPFF LSFTLPYSAV RGERIPIRVT VFNYLEKCLL MEIKLNLWGG
IEIVQGSYQN KPFCLCGGKS HTTKYYIVPT EIGELPITAI AEILPGSCDN SVEMDLNYIG
MRDAAERNIL VKAEGVQQEY SLSRYICLDS GKDEVVEQFD LQLPEQWVDD SARGEFTVIG
DIMGPALSNL DNLVSQPTGC GEQTMVTFTP NIYVLKYLQS VQQDTEELEA LAKNYMEIGY
QREMTFRHDD GSFSAFGKSD KSGSTWLTAF VIQSFAQARE FIYIDTKDLE KSIKFIRTRA
RLENGCFREV GKVFSSYMMG GLDTSKDSSL TTLTAYVLIS LLEANVSKED PMIIEGMNCL
NAQEPTEDVY TMSVLTYANV LYNVNSTESV EALDRLNEQV IKNGNIEHWA RKGPKPKPVN
SWYYFVAPSA EVEMTAYGML SRLHSTDNIG DVVPLAMWMS QQRNSFGGYA STQDTVVGLH
ALSEFAAMLK QDGNGETTEG LKILFQGKSQ ENSLNVTSEN ALLLQTVNLK ELSNFFDVTA
RGQGCALVQA NVRYNIDPDD LDTGKIFALK VSARREENDC ALKAMEICVS FYKHQGYSDG
MSLVTVSMVT GWSVEPKSLK RLRSRFSMLN MKKYEIDNTD GSINFYFDEL DHRQRCFKFD
LIQNKDLAVS SPKSGIVKVF QYYEKEVSEV KSYSLKTICG TKEEIPIKPP QVLPPIDEPD
FIQRRVFDVR GSGDDSPIVP ERVNPLTRLR EVPSPRKNIK CPVCTNTPPD NLDDLVCQSG
SILKVSAGRN GRVTMKLKAD LRPRRKQRLD EFVSVDLNSQ CPCNLIKPPK RQKRVKRLLV
FTESPNLFDK EGQKEKAFDL TKAKYVINLD LDKKLERRVR LLARKCRTP
//
