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Database: UniProt
Entry: G1PPU5_MYOLU
LinkDB: G1PPU5_MYOLU
Original site: G1PPU5_MYOLU 
ID   G1PPU5_MYOLU            Unreviewed;      1577 AA.
AC   G1PPU5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=C3 and PZP like alpha-2-macroglobulin domain containing 8 {ECO:0000313|Ensembl:ENSMLUP00000013050.2};
GN   Name=CPAMD8 {ECO:0000313|Ensembl:ENSMLUP00000013050.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013050.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000013050.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000013050.2}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AAPE02039116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02039117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02039118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02039119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02039120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000013050; -.
DR   Ensembl; ENSMLUT00000014345.2; ENSMLUP00000013050.2; ENSMLUG00000014332.2.
DR   eggNOG; KOG1366; Eukaryota.
DR   GeneTree; ENSGT00940000162399; -.
DR   HOGENOM; CLU_001634_1_0_1; -.
DR   InParanoid; G1PPU5; -.
DR   OMA; FIRECCT; -.
DR   TreeFam; TF313285; -.
DR   Proteomes; UP000001074; 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   GO; GO:0001654; P:eye development; IEA:Ensembl.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 2.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 6.20.50.160; -; 1.
DR   Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR022041; Methyltransf_FA.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR041555; MG3.
DR   InterPro; IPR040839; MG4.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412:SF139; C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 8; 1.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF12248; Methyltransf_FA; 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; 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:UP000001074};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1577
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003418188"
FT   DOMAIN          454..623
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          747..838
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          504..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1510..1530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1577 AA;  174233 MW;  0158965DC87F74A6 CRC64;
     MWGALLGPLL GLLLLLSPRD SVHAARPQAP GYLITAPSVF RSGVEEVISV TIFNSPREVM
     VQAQLVAQGE AVAWSQGAML DKGTIKLKVP TGLRGQALLK VWGRSRQEEE GTLFHNQTSV
     SVDARGASVF IQTDKPVYRP QHRVLISVFT VTPDLRPISE KLEAYILDPR GSRMMEWRHV
     EPVCCGITNM TFPLSDQPVL GEWFIFVEMQ GHVYNKSFEV QKYALPKFEL LIDPPRYIRD
     VDACETGTVQ ARYTFGKPVS GTLTINMTVN GVGYYSQEMG CPVLRTMKIH GSQDFHICVR
     DMIPTDIPEH FRGTVSIWAA VTATDGSQQV AFDDSTPVQK QLVDIRYSKA TRKQFKPGLS
     YMGMVELTYP DGSPAEGVTV QIRAELTPKD NIYTTESVSR GGLVAFEIPS IPTSAQHVWL
     EAKVTALNGK PVGTQYLPSY LSLSSWYSPS QCYLQLQPPA RPLQVGEEAR FPVTSTCACN
     LTLHYEVAAR GNIVLSGQQP ARITQQRSRR AAPEEPIRLT HLSETEPPPA PAAELSVCMT
     SLQLSVTPSM VPLSRLLVFY VRENGEGVAD SVQFTVETFF ENQVSLTYSA NETQPGEVVD
     LRVRAARGSC VCVAVVDKSV YLLRSGFRLT PAQVFQELEE YDVSDAFRVS WEDGPLWWAG
     LAARRRRRSF VFLWLWGVIK DSGFAFAETG LVVMTDLVSL NHRQDGGLYT DEAVHTFQPH
     TGSLMAVASS RQPPRAEKRR RTFFPETWVW RCLNISDPSG EETFRVQVPD SITSWVGEAV
     GLSSAWGLGI ATPSLLKTFK PFFVDFTLPP QVVRGEQVKI PLSIYNYMGT CAEVYVQISV
     PKGTRFVGHP GKRHLTKKLC VASGETEPIW VVLSFSDLGL SNITAKVLAY GETSCCRDGK
     PSKQAEESYA DRVPAGRDHI RRSVIVEPEG APRTYTYSAF FCPNERVHIS TPNKYEFQYV
     QRPQRLTRFD LSVRAHNDAR VALSPGPQDA AGMIEIVLGG HQNTRSWIST SKMGEPVAGT
     HTAKILSWDE FRTFWISWHG GLIQVGYGPE PSNESVIMTW TLPKAPDVQF IGFSTGWGSM
     GEFRLWRKME VDESYSEAFT LGVPHSAIPG SERAAASLIG DVMGPTLSHL SSLLRLPFGC
     GEQNMIHFAP NVFVLKYLQK TRQLSPEVER ETTDHLVQVR ERERERERES RSLSWGTRGP
     FTSRWLTAFV LKSFAQARSF IFIDPRELAA AKGWIVRQQQ VDGSFPATGR ILNKDIQGGI
     HGAVPLTAYV VAALLETDVA SEVSTGAPRD QAGGTGEGFP LLACAGQAWV WVPCCAIPGA
     CPGRWEAWGE LPSAIFMTLN NSHWGVAGGG ECEQGWWALW RRRTLIRGLE AEKSGAVGLR
     GQRGDEGGGW AGSALPVSSE LLWDDMMCSD FIRECCTLNA TSGVHAEYRR ESPGGGQTWL
     KPCKKNRADV TVVVILASPT CPCLAPPTPH THTPRAPRLG LLTPQIDVSY NVPDPVAKPS
     FQLFVNLQEP EAERPRPPAP APSADDDDPA ADLHHQEYQV TLEVCTRWLH AGSSNMAVLE
     VPLLSGLRAD IESLEQV
//
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