ID F6TCS3_XENTR Unreviewed; 1482 AA.
AC F6TCS3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Alpha-2-macroglobulin {ECO:0000313|RefSeq:XP_002938549.2};
DE SubName: Full=Pregnancy-zone protein {ECO:0000313|Ensembl:ENSXETP00000052286};
GN Name=LOC100489060 {ECO:0000313|RefSeq:XP_002938549.2,
GN ECO:0000313|Xenbase:XB-GENE-29079547};
GN Synonyms=pzp {ECO:0000313|Ensembl:ENSXETP00000052286};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000052286};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000052286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000052286};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000052286}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002938549.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002938549.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002938549.2};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_002938549.2; XM_002938503.5.
DR STRING; 8364.ENSXETP00000052286; -.
DR Ensembl; ENSXETT00000052286; ENSXETP00000052286; ENSXETG00000024227.
DR GeneID; 100489060; -.
DR KEGG; xtr:100489060; -.
DR AGR; Xenbase:XB-GENE-921402; -.
DR Xenbase; XB-GENE-29079547; LOC100489060.
DR Xenbase; XB-GENE-921402; pzp.
DR eggNOG; KOG1366; Eukaryota.
DR HOGENOM; CLU_001634_0_1_1; -.
DR OMA; NYMSHCI; -.
DR TreeFam; TF313285; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Bgee; ENSXETG00000024227; Expressed in liver and 5 other cell types or tissues.
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:SF150; ZGC:171445 PROTEIN-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:UP000008143};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041199123"
FT DOMAIN 453..602
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 752..842
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1379..1467
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1482 AA; 164186 MW; 77002CA4C619BD2F CRC64;
MWSCALTLCL LLTAFPGGDP APPDPQYLLL VPTVLHGASE EKFCLLLSHL NETVTMTLTL
YLPTQNHTLL EKQVTEKEED GCVTFMTPKL EVAAVAILTL DVQGDALHFK SQRKILIKPL
QNPVFIQTDK PIYKPGQKVQ FRIASLDENF HPVSEKFPAV YITDPQGNRI SQWLNVELKK
GLTQESFQLS SEPTLGIYKL TVGREKSAPV THSFSVEEYV LPKYEVQVKL PPVVGIMDKG
IKVTVCGRYT YGKPVLGRIK VRVCRKFSDR YNLCKGEEDG VCEEINHRAG PNGCFSEVVS
TRMFQMRRSG YEDKIRASAT IIEDGTGVEL TAAVSSEIKK TLAKVSFRHL DSHYRKGLPL
FGQLFLEDAS GNPMANETVV IFVGYGTNFT YTTGQDGTAE FLIDTSNVQK SSLQIRARYK
EGESCYQYRW VSVSYQGDER SVKEFYSRAK SYLKIQPIYK ILECQKQEKV IVHFILSAEG
VGETTNAVFH YLVMSKGGIA GHGRHEIEIS PNQNASGTFW FRLTAGTDIA PSANFLVYLI
LESGEVIADS ISLKVEKCFG NKVELSFSPS EALPGAPADL HLLTAPSSLC ALRAVDESVL
ILKPEAELSA QTIYNLLPLQ DLSGYIHDGN FLEELWDDPC IKMEPLFING IYYMPTNPEW
DTDTYTILKN LGLKVFTNAR IRPPLVCGPR SFYEHYGTGG PFAVPMSLSA GMGVQAGMGV
QAGMSGAGLH IGRNIPVAEP VIETVRKYFP ETWLWQLVET DADGKADLAV TVPDTITTWK
AGMFCTSQGA GFGLSETISL VAFQPFFLEL TLPYSAIRGE IFTLKATVFN YLSQTIRVGI
LLEDSNQFLA KPTKVQEDGY CVTANGQVTL SWEVTLKSLG EVNFTMSAET LNGEGLCENE
IVSPAQGRKD TITKHIIVEP EGVKKEETHS TMICGKGSEI TENIPLKLPE KVVEGSARAY
FSAVGDILGT AMQNLGNLVQ MPYGCGEQNM VLFTPIIYIS EYLNKTNQLT PEMKSKTLSY
MSTGYQKQLS YKHPDGSYSA FGQRYGEGNT WLTAFTMKSF ARARAHIYIE EKLITGALLW
LSIRQKPNGC FHSVGKLFNN AMKGGVDDEV TLAAYITIAL LEYPLPVTHP TVRNALFCLE
SALGGKNGIY TKALMAYAFT LAGRMDIRRQ LLQSLDEQAI KKDGTVHLHR PEFSDDSGVD
RFPYRRAPSA EVEMNSYMLL ALLSKHNVSD EDLTLATQVV SWMIKQQNPN GGFSSTQDTV
VALQALSLYG SLTLSHDAMR TVSLSLDKTP VAEFHVEDSN RLLLQRIALK EVPGDYLATV
SGSGCLYLQT TLRYNVPIPK EDAPFTISVT TDPETCDRKS LKTFTIVANV SYVGKRLNSN
MAVVEVKLPS GYIPIKPSVK KMTASNRLIQ RAEAHANEVI VYFESLFKDI QSFRFSVEQE
IPIGNLQPAT VVVYDYYETD DLAITKYDAP CSAKDGANKE QQ
//
