ID A0A3P8S2Q4_AMPPE Unreviewed; 1487 AA.
AC A0A3P8S2Q4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Alpha-2-macroglobulin-like {ECO:0008006|Google:ProtNLM};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000006325.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000006325.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000006325.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 161767.ENSAPEP00000006325; -.
DR Ensembl; ENSAPET00000006494.1; ENSAPEP00000006325.1; ENSAPEG00000004553.1.
DR GeneTree; ENSGT00940000166660; -.
DR OMA; PEKGRMD; -.
DR Proteomes; UP000265080; Chromosome 9.
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:SF160; ALPHA-2-MACROGLOBULIN-LIKE PROTEIN 1; 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:UP000265080};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1487
FT /note="Alpha-2-macroglobulin-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018235546"
FT DOMAIN 456..606
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 769..858
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1386..1474
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1487 AA; 164083 MW; C7E361A8C3D5488A CRC64;
MAPVLQMFAV TLAAALLQTA TSAHLNDTIF AVTVSSRVTA GNQETLCALI HGPTEPISLN
ITLNTEFGNS VILEEDVKED FYRCLSFQVP TVPRRTVASI HVTIQGENAS LGKKTKVLVE
PPAFIHVVQT DKPIYKPGQT VQFRIVSLDA NFIPVSRVYK EVALQDPNSN RIAQWLDKAI
VSGILDLSHP MIPEAVQGTY TITALTDKGE QISHSFDIKE YVLPKFEVNV KLPSVITILD
EEATLRICGK YTYGKPVIGS VKAEFCRRAV RYWYVVRSTD NDICKTYHLT TDKSGCATQT
VNLTAFALDK TMYTDSFQVS AEMEEYGTGV ILKGNGRTTF NSHIRTASFE DVPAAYKPGI
PFEGKIKVVG PDNKPASNEP VYLSAGDLQK LVLTTDRKGV ALFSLDTSLW KDSVYLVASS
KNTTDHHPYV HNLRRAEYRS AHHHVTPFYS KSSSFLKVMQ VNGKLSCDKD TAVRAQYIIQ
GDELKKGQEV LDFFYLVLSR GAIVLHGHVP VTVKAGTVNK GQLSVPLSQM TNLAPFAQVV
VYTVMPSGEA VADSLDFPIQ LCLNNKVSLK FSSLQELPAE KTTLSLQAHP GSMCSVRAID
QSVLLLQAEQ ELNVGYMYSQ LPVQKLSGYS YEVDDFEPYP CFPMPVPEPE IEIAPESTAA
PTAVPAPDTV PDAQAIRRAT RSLFFGNSDQ KNDVYSIFKE IGIKIMTNSD VKKPYDCRER
AYEYFLYDAD VVDSPVPMAF NMMPQNSGFV LKEKEEEKKK TVRTFFPETW IWDLVPVGDS
GAVDVEKTVP DTITKWAAGA FCVSSVGFGV SPNTGLTVFQ PFFVSLTLPY SVIRGEVFTL
KATVFNYLSK CIMVKVTLDD SDQYTFRNCD GCHYTICLCA EESRTFSWIV TPTALGKLNL
KVSAEALKTD TLCGNEVATV PDVGRVDTVI RTLLVEAEGT PQMISHNALL CPTDGPVEKK
ISLLMPEMFV AGSARASVSV LGDLMGRAMK NLDKLLEMPY GCGEQNMLLF APNIFILNYL
KSTGQLTQKI LDKATHFLES GYQRELTYKH DDGSYSAFGK SDASGNTWLT SFVMKSFGGA
RPYIYVQPQH IKDARRWLSK HQRPDGCIRS VGKLFHNGMK GGVSDDVSLT AYITAALLEL
DADATDPVVQ NCLSCLKAAV AGQLDNLYTT ALLSYTFTLA GDQDMRSKLI TTLHQKSNTQ
GGTRHWERVG ASKKVLDSLE VEITSYVLLA LLSGPAMPDF GLDYSSGIVR WLTQQQNPYG
GFASTQDTVV ALQALAKYGA ATYSPEGSTT VTVTSLGGLN KGFTVDQSNR LLYQEEKLSE
VPGEYTIKAQ GQSCVLAQIS MHYNIPPPAD FSAFNISTNT MAKCNISRPQ LILFVHVRYQ
GRREETNMVI ISIKLLSGYI LDKSSLSLLQ RDRSVKRVDL DEGFINIYLD GLKKAETQIY
SVTLEEDQPV RNLKPAVVKV YDYYQTSDEA VTDYTSACAE SDTINEL
//