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Database: UniProt
Entry: A1L1H6_XENLA
LinkDB: A1L1H6_XENLA
Original site: A1L1H6_XENLA 
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
//
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