ID F1A2X2_DICPU Unreviewed; 2080 AA.
AC F1A2X2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0000259|SMART:SM01360};
GN ORFNames=DICPUDRAFT_99830 {ECO:0000313|EMBL:EGC29461.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29461.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; GL871429; EGC29461.1; -; Genomic_DNA.
DR RefSeq; XP_003294015.1; XM_003293967.1.
DR EnsemblProtists; EGC29461; EGC29461; DICPUDRAFT_99830.
DR GeneID; 10505330; -.
DR KEGG; dpp:DICPUDRAFT_99830; -.
DR eggNOG; ENOG502S0ZT; Eukaryota.
DR InParanoid; F1A2X2; -.
DR OMA; ANITDNC; -.
DR OrthoDB; 6503at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1930; -; 1.
DR InterPro; IPR041246; Bact_MG10.
DR InterPro; IPR001599; Macroglobln_a2.
DR PANTHER; PTHR13062:SF9; A2M DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13062; COLLAGENASE; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF17973; bMG10; 1.
DR SMART; SM01360; A2M; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1355..1446
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 2080 AA; 234026 MW; C54279110B33B991 CRC64;
MVSLKIPIII LSTLIGILFI FSYINNNNDI QLNQAYQQYN NNNNNQQQQR HLNSYNEKLS
LQSPAFLNIS VVDKHNDQNF EDGNIQKIKV PLNLLNIFPT DGSLRNIDPI TVVFNRPVVP
LGEISTYFPF KLQCKGNLVP IEGDYRWVTT SIARFDIRGK WPSNLQCTFS VDPNIKCFDG
TTLTAPLSSS SPPMFISFST SKPSITIDSV VSEKTSNFTN NQWSSFYTFN DTGYYEVPPD
GIIKFSVDEP FDTSSIQKSL IIYLSSSQNL KNKNLITYSI VKCPNEDDYY LSTNYYFCIK
ASRLETSKFY KAEFKRGTRL NLKSGPLGES IYSEFSGLRE FKFYFHNKEL SNVNQKLSIL
HGLPKTFSNG QLLTSMISFT PQLSFTSKLD IKDSSILLLI SNLEYGVNYT IRVKGNQKIL
DGWGLPLKDA VWNFTMSTVS SLQVTYGLSD FSKDDKGEKE NLYTFHQNSI YHGYYSYGDQ
KCSNLEEPRK VLGYPITKAN LIDCIKSYSS GQLMLTEKPK KTVVFDEPSN TTLFQSYLPN
KSLWKPTGVY LKAELHSVDY YSCNPNYKID FVSNTDVGVS FLTVTPNSIG LWVTRLSDGS
NLKDVSVSFY NINQKYSSTT SKTTTEVLLV GTKKTSAIGT VDFKTNNTNG MAVIEYDGDR
LFIAKTDSLY RSYYYPVSTS AVIVTDRKLY NGGEKMYIKI YLSGEHNIYR FTIKIRWNVL
DSINEFSQLV DIDDNYGTAD LSVNIPDQVK MGPYSIILQG QNTVSDSSSD ITFYESILIS
DPRIPSGVLS ITPNQRYLQY SSSYTSLSAS FSINTNTYLG VPLPNKNVSI SCSFSRNSIN
SRSFSFTETK SIFTNNDGFA SLEFTFDRKN VQFEDGDIIT CSGSYMDSTG SLISQDSPMV
ISILSSEYSL QIRSESSVTR GYPSTVNVLL LNQTTFEPIK NIPIDVRIVE SNTNPYDYQG
KTIKNSIFNI WDSGKKKSLT TSCHYETDSS NTDKCYIVLP EEESPTATIY YLVVKASLPD
GTELKNYKKI SVDYEYKAGE DGVSAKGFLN ENAKVFSIPD SLLWFTMDNE VYYPNQTVDV
RFYNPFKMGT MTFKFGCGSK NQYEKQISKP HGFQTLSISI PSDCGGKTLS VVGTLIGTKY
GFKISDSIPT SLTKYNPDKP NPQTFSLSYR INQQKDLEIS IDLDDSIFKP NEQASFSIKV
ADPNTKKLID EQVEACIMVV DKRNYDLYGN PIESGEKLSL DSPFREISDT RFNLIHNYRE
QVRIVEKILS NNKWTYFGWD RYSQISKNSS LFSFYQYEWF TERSQNSIFF KSFNTFAPSA
RQFDDEVADA SPLMGTGANG AQSNQAIIKT NYQTTPLFIG KSLISNGLVN VSFTLPDDLT
TFIIRVYIIN KESQLYSKES SLISRKDLNM IGFSPRFVRT DDQFESGVSI TRLSESIDVS
DLCVAAKYKE PCIQFDSKDK VPTKDLVFND NSRLSTNIMF SLTAEYQCDT ATLYFFLQKK
SSGEILDQIT TKFAVLGKQA PLYVGTSFQV KANSTSEELL SLPKSEGDIG SLKITVGVGH
LPVVEEKSMR LLSINKNRLP SSIDLLSQQV TYGALSSYSY NSSLIVMSQQ IIESINEGFY
AYTSSDYISW YPNSQPDFYP NLYATVLKGI MDVTNTAGWS IIGNISNWSS FVDQQLNSNL
QDAVKNNRSI DKETIGLASI GFGYYWAPKD EDLNDLYSFN ALTSNITDNC SLLCQTYFAL
AAIIREEYTS PFIGQVIDNL KNNIRIQGRT AYIESEGINN NPFYSLKLTT YASILFILRN
ESSPILPKMI EFISVGSSGS NGLSYFPIEP SSESQALSLI AISFYDRVNE NTSPDLEFSA
YQSNYPPIIQ HHFYPNNNDS VEKVVPFNSL ESNQTIQFNS KGTGEVSVAV GINYTPINIP
TTPVYNGFYV EKIVSEYSYS TPSSSPATPI NSSNEFYVGQ EVMVTISVTV PDYMRDVYIE
DGASGGIEPI DNNLDNSGDG PTPYYREPSL IWYYQPFSHR ETRKEKVIFQ GSNIIAGSYT
VSYKCTVTSK GTFTMPPAKA YSSIQPEVFG TSNGFKYKVL
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