ID L5L670_PTEAL Unreviewed; 1925 AA.
AC L5L670;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Complement C4-A {ECO:0000313|EMBL:ELK18900.1};
GN ORFNames=PAL_GLEAN10001061 {ECO:0000313|EMBL:ELK18900.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK18900.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB030277; ELK18900.1; -; Genomic_DNA.
DR STRING; 9402.L5L670; -.
DR MEROPS; I39.951; -.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; L5L670; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd02896; complement_C3_C4_C5; 1.
DR CDD; cd03584; NTR_complement_C4; 1.
DR Gene3D; 1.20.50.70; -; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.1540; -; 2.
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; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR048847; C4_MG1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR018865; STK19-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF86; COMPLEMENT C4-A-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; PF01821; ANATO; 1.
DR Pfam; PF21145; C4_MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF10494; Stk19; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
DR SFLD; SFLDG01179; Complement_C3/C4_Like; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 4: Predicted;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT DOMAIN 882..916
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1776..1923
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1516..1543
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 84..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1925 AA; 212601 MW; B2050FD6C0F47D58 CRC64;
MSRKRQRLVP ETLGLKRWRE RGHAEADPLR GEAGSARAAV TELVGLFPRG LFEDALPPIA
LKSQVYSLVP DRTAADRQLV RGASATDRSR TQNPQSKALQ EQGEIRIIQL GFDLDAHGII
FTEDYKNRVR AIVLKACDGR SYAGAVQKFL ASVLPACGDL SFQQDQMTQT FGFRDTEITQ
LVNAGVLTVR DAGSWWLAVP GAGRFIKYFV KGRQAVLSMV RKAKYRELLL SELLGRRAPA
AVRLGLAYHV HDLIGAQLVD WLLLFSPSVV HLGVPLSVGL QLQDAPQGQV VKGSVFLRNP
YKLNVPCSPK VDFTLTSEKD FILLNVQMHL RGAESCGLKS LLGGPEVQLV AQSPWLKNTG
SKEIDIQGVN LLFSSRRGHL FLQTDQPIYN PGQRVRYRVF ALDQKMRPST DTITVTVENS
HGLRVRKREV YASSSIFQDD FVIPDISEPG TWKISARFSD GPESNRSTQF EVKKYVLPNF
EVKIIPGKPY ILIAGGILGE IQLDIQARYI YGKPVQGVAY VRFALLGENG DKTFLRGLEN
QTKLVDGQCH ISLSKAEVQG ALAKLNMHLT DLPGLRLYVA AAIIESPGGE LEEAELTSWH
FVSSPFSLDL SHSKRHLVPG TPFLLQVSAG SPYPATAMLT VRAPPSRSSG FLSIERLDSR
PPRVGDSLIL NLRDVGVSGA SFSHYYYMIL SRGQIVSVNR EPRKTLTSVS VFVDHHLAPS
FYFVAFYYHR GLPVANSLRV DVQAKACEGK LELNVDGHKE YHPGDTVKLH LLTDSPALVA
LGAVDTALYA VGGRSHKPLD MGKVFEVMNS YNLGCGPGGG DNALQVFEAA GLAFSDGNQL
TSARKSLSCP EEKKTRKKRN VNFQKAIFEK LGQYTSPIAK RCCQDGLTRL PMPRSCEQRV
ARVQQLACRE PFLSCCQFAE GLRKKIRARG QVGLARALEI LQEEDLMDED DIPVRSFFPE
NWLWRVATVD RFFQLSHLLP DSLTTWEIHG VSLSKSKGLC VATPVRLRVF REFHVHLRLP
ISVRRFEQFE LRPVLYNYLD KNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVGFS
VVPTTAAAVS LKVVARGSSE FPVGDAVSKV LQIQKEGAIH IEEIVYELNP LDHRSRTLEI
PGNSDPNILP DGEFSSYVRV TASDPLDTLG SEGALSPGGL ASLLRLPQGC GEQTMVLLAP
TLAASHYLDK TEQWNKLPPE TKDHAVDLIQ KGYMRIQQFR KTDGSYGAWL HRDSSTWLTA
FVLKVLSLAQ EQVGGSPEKL QESTRWLLTQ QQADGSFQDP CPVIHRGMQG GLVGNDETVA
LTAFVVIALH HGLAVFQDKN AEELKQRVET SISKANSFLG TKASAGLLGA HAAAITAYAL
TLTKAPEDLQ NVAHNNLMAM AQETGDHLYW GSVASSQSNV VSPTLAPHSP ADPVPQAPAL
WIETTAYGLL HLLLREGKAE MADQAAAWLT HQGGFQGGFR STQDTVITLD ALSAYWIASH
TTEERDLNVT FNYTSRSGAK SHVLQLNNQI QGLEEELQSS SGSKINVKVG GNSKGTLKVL
RIYNVLDMKN TTCQDLKIEV TVMGHVEYTM EANEDYEDYE DYEREILAGD DPGPLSQPVT
PLQLFEGRRS RRRREAPKVA DEQESRVQYT VCIWRNGKVE LSGMAIADIT LLSGFHALQA
DLEKLTSLSD RYVSHFETEG PHVLLYFDSV PTSRECVGFG AVQEVAVGLV QPASAALYDY
YNPEHKCSVF YGAPTKSKLL STLCSADVCQ CAEGKCPRQR RALERGLLEE DGYRMKFACY
YPRVEYGFQV KVLREDARAA FRLFETSITQ VLHFSKDAQA TAGQTRNFLV RASCRLRLEP
GKEYLIMGLD GATHDLKGHP QYLLDSNSWI EEMPSERLCR STRQRAACAQ LHDFIQEYST
QGCQV
//