ID A1L1H6_XENLA Unreviewed; 1457 AA.
AC A1L1H6;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=LOC100036845 protein {ECO:0000313|EMBL:AAI29065.1};
DE SubName: Full=Uncharacterized protein LOC100036845 precursor {ECO:0000313|RefSeq:NP_001090602.1};
GN Name=LOC100036845 {ECO:0000313|EMBL:AAI29065.1,
GN ECO:0000313|RefSeq:NP_001090602.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI29065.1};
RN [1] {ECO:0000313|RefSeq:NP_001090602.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI29065.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocytes {ECO:0000313|EMBL:AAI29065.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001090602.1}
RP IDENTIFICATION.
RG RefSeq;
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 EMBL; BC129064; AAI29065.1; -; mRNA.
DR RefSeq; NP_001090602.1; NM_001097133.1.
DR DNASU; 100036845; -.
DR GeneID; 100036845; -.
DR KEGG; xla:100036845; -.
DR OrthoDB; 5311636at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 100036845; Expressed in zone of skin and 13 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 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; 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:SF173; ALPHA-2-MACROGLOBULIN-LIKE 1 PSEUDOGENE; 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 2: Evidence at transcript level;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001090602.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1457
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001090602.1"
FT /id="PRO_5033207201"
FT DOMAIN 459..603
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 735..826
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1363..1449
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1457 AA; 161010 MW; 3BEE7DAC48CCC047 CRC64;
MNQRRFLLFS CLLGLIAGAT SKLHHVLTIP VQLSSGGTQR ACVNLQDYEE AVSLHVVLLH
NGVETTIFEE TVQPPCFFMC KEFPVPEVES DTPVAVTLSA ISGEEEVLDR KTVVIVSQQK
TQTVTFIQFD KPIYKPGNKV DFRLITMDSL LHPVNQQFSA VYLQDPSGSR IAQWLDLTSQ
RGVAELFFQL ISDAAPGSYN IIIESTPDSI DVMEYFTVEE YIPPRFSVSV AAPQTLSVLD
ETAKFNVSAV YTYGQPVPGR VTVRICKQVF PFGRSQNCLK DKSEKCLDTS EQLGPDGTYQ
AEIDLNPLSI GLSVFGSSLS VDITVVEEGT GVQVRENRYI GISSQLASLS LDYESLQQYY
KRGLPYVLRV TLINEKGQPL VNEKVDLEIQ SSVIQEVNTD QAGKAEFQID TSSFAMPNFT
FKVSYQNPAL CYYSQWENTN YPSVEYQVLR FYSESGSFLQ LYGPKEALSC GKSYSINVQY
IVNCDKAGDT ATFFFLVMSK EKIVLSGAQD VDVTTSKNGS ISINIDVTSE LVPSARVIVY
SILHSELIAD TVTLNIETCF KHQVSLSFSE DRGPPASNVD LKISAAPGAF CGVRVIDSSL
LLLNSYERFS ASNVYSSIPY LSFYGYNVGE LDLEEPKPPC EDPHRQIFYN GSYYIPISSY
SEGDSYGIFK QLGLVVGTEY RLRKPVVCGY EQEPIVPIRK GGFGGGFGGP MLTSVLADGV
GTGRIETVRK DFRETFVWKM VVVDSEGKLS FTEKVPDTIT EWKGSMFCLS EEQGFGMTTY
TANYTSFLPF FVEPSLPYSI TRGETMVLRA FVSNYLQKCI TISVTLAESA DFEAAPQDVQ
QDKCICAGGR ATYSWNVDAK TLGEISFSLS AETTNIGDTC EGPNDPSQPL RKDTVIRTVL
VEAEGIRREV TSSNLVCVDG SNTEIPISIT PPENIVSGSA DGYIIALGDV IGLPLSNLQN
LLQMPYGCGE QNLARLAPIP DVLDYLNNTG QLTDKILQTG IKFMTEGYYR QTRYKLWNGA
YSTFWGWAAQ SNSWLTAYTF KTLEKCKKYI FIDKNIQQQT LIYLEQRQKL ESGCFMPEGQ
LFIKEDEKDE EAISVQYTAF LAIALLESNY SLGKTLLDGA MGCLRNASTR EQKMINKALM
LYAFTLAGDE EHRASLLEAV KQSAVSEGGS LHWEREGTTG NVAVPFFYPR HAAANVEVTA
YILLSIAKGS IVTQEDLTYM AQIAVWLIRQ QNSFGGFRST QDTVVALQAL TSYGRLIYKP
NANHNLAITS GNDGVGQMTL NQSNRLLVQR QPLPEVPGEY GVGVSGTGCC LIQSTVRYNI
PVPDENSAFS MSATSSGNCL DGVATLVDLT LQVSYQGNRD APSTVIIDVK LLSGYQADYL
SLYELENAKL IARFEEKNGH VILYLNSISS EPVDLTFKMQ MGSRVLNVMS SSVYVYDYYE
ADENGYASYS HPCPVAT
//