ID F4W4T0_ACREC Unreviewed; 1432 AA.
AC F4W4T0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=CD109 antigen {ECO:0000313|EMBL:EGI70799.1};
DE Flags: Fragment;
GN ORFNames=G5I_00405 {ECO:0000313|EMBL:EGI70799.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70799.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL887553; EGI70799.1; -; Genomic_DNA.
DR STRING; 103372.F4W4T0; -.
DR EnsemblMetazoa; XM_011053241.1; XP_011051543.1; LOC105144368.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; F4W4T0; -.
DR Proteomes; UP000007755; 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 CDD; cd02897; A2M_2; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 2.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 2.60.40.2950; -; 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:SF176; GH01829P-RELATED; 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 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT DOMAIN 422..557
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 688..779
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1306..1395
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI70799.1"
FT NON_TER 1432
FT /evidence="ECO:0000313|EMBL:EGI70799.1"
SQ SEQUENCE 1432 AA; 160227 MW; 7C6E4A4F910752D4 CRC64;
RYYTIIAPKV VRPDSEYHVA ASVTGVSTPS TIYVELTGEL DIGKIFNISR TIVVEPYSTH
ILQLNIGETT PGKYKLTARG LSGIDFYKSK DIEYVHKSYS VFIQTDRAIY KPGHKVMFRC
IILDSRLRPS IMRPSDVYVI DGDGNRVKQW NRPPVTHGIF GSELELSQSP VLGKWKLVAN
VGDQTFEKEF EVAEYVLPNF EVTIDSPKHV QFKESKIAAT VHAKYTYGKP VKGEATITAY
PDIFSGVIQP IFQQPVRKVV PINGKVTVDF DILSELRLTD EYERPIMIDV VVEEELTTRR
QNASTQITLH KHKYTMELIR TSDYFKPGLK YTAFLKLTYH DGSPVQDTKN DVLIAYGYTY
NQSAYSNLTK KLDEHGMIQL DFYPPKSKDN ISFPLNIEAQ YLNLHEWFPS TSQAMSISNE
YVQAILKTEK PMVNSYVEIE VNSTAPLKYI SYEILGRGDI LDAGSIYVQD KYTTSFKFLA
TYVMAPIAHV IVYYVGTDGE VLADSLDVEL TGVLQNHVDI KITPGEVMPG ENVNLMISAK
PNSFIGLLGI DQRSLLLKSG NDISYDQVYK ELQTYDKAEP SPHADGFFSR SLWRPGSGTA
DDVFQKTGVI ILTNGYVHEN FPVRPEILEG RITGSPHGVS TLRPDLGPPV THRLATRPPL
AGPYAFSRIP PPVWNKPRVF LMHDILNTWL FTNFSSGYNG KTELRREVPH SITSWVLTAF
SVNDAHGLGL IEEPRKLKVF KPFFISVDLP YSVIRGEIVS IQIVVFNYMN KDLTAEVLLT
NDGQFDFAEV SNEVHDAPKL ELYRRKKVDV KANSGSSVSF MIIPRELGYI NIKATANSVL
AGDSVEHKLL VNAEGETQYK NKAVLLDLRS AAQASANVTI DIPNNAVPGS EIIQISAVGD
VLGPSIQNLA NLIRMPFGCG EQNMLNFVPN IVVLNYLKNT NQLTQAVQSK ALKYLDIGYQ
QELTYRHTDG SFSAFGMSDP SGSTWLTAFV AKSFKQAAEY IAVEDRIITE ALQWLSNNQA
SNGSFPEVGK VSHRDMQGGA AKGLALTAYT LIAFLENEES VVKYRNTINK AVDYIVRNME
GLNDTYALSL CAYALNLAKH PYETSAFNFL ESKAVMNQDL KWWSKPIPKD NKNPHYSLPR
SVDVEMTSYA LLSYLKRNLV TDAIPVMKWL VRQRNTEGGF ASTQDTVIGL QALAKLAEKL
SKDTSSVEIT YKYGEGEGQE GYMNIRGDNS IILQKKMLPT KTRYVNITAS GKGFVLVQVS
YQYNLNVTGA FPLFTLDPQV DKNSNANHLQ LSICSGFVPT EEANESNMAV MEVSLPSGFT
VDRDSLPSLE MSSHVKRVET RNGDTMVILY FDKMIKQEYC PTVSAFRTHK VAKQKPVPVS
VYDYYDSSRR ARAFYEPKKT TLCDLCEDED CEDICVSKPG KRKDNTTASA AS
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