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Database: UniProt
Entry: A0A2K6DNL1_MACNE
LinkDB: A0A2K6DNL1_MACNE
Original site: A0A2K6DNL1_MACNE 
ID   A0A2K6DNL1_MACNE        Unreviewed;      1698 AA.
AC   A0A2K6DNL1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMNEP00000037498.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000037498.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000037498.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   Ensembl; ENSMNET00000061965.1; ENSMNEP00000037498.1; ENSMNEG00000041718.1.
DR   GeneTree; ENSGT00940000155739; -.
DR   OMA; DYMNSYD; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000041718; Expressed in liver and 8 other cell types or tissues.
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; 1.50.10.20; -; 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; -; 3.
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; 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; 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; IPR040839; MG4.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
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; PF17789; MG4; 1.
DR   Pfam; PF01759; NTR; 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   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:UP000233120};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1698
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014419510"
FT   DOMAIN          702..736
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01178"
FT   DOMAIN          1549..1696
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
SQ   SEQUENCE   1698 AA;  187658 MW;  2253C262B9062CE4 CRC64;
     MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVPRGQ VVKGSVFLRN
     PSHNNVPCSP KVDFTLSSDR DFALLSLQVP LKDVKSCGLH QLLRGPEVQL VAQSPWLKDS
     LSRKMNIQGV NLLFSSRRGH LFLQTDQPIY NPGQRVQYRV FALDQKMRPS TDAITVTVEN
     SHGLRVRKKD VYLPSSIFQD DFVIPDISEP GTWKISARFS DGLESNRSTQ FEVKKYVLPN
     FEVKITPGKP YILTVPGHLD EIQLDIQARY IYGKPVQGVA YVRFGLLDED GKKTFLRGLE
     SQTKLVNGQS HISLSKAEFQ DALGKLNMGM TDLLGLRLYV AAAIIESPGG EMEEAELTSW
     SFVSSPFSLD LSKTKRHLVP GAPFLLQALV REMSGSPASG IPVKVSATVS SPGSVPEVRD
     IQQNTDGSGQ VSIPIIIPQT ISELQLSVSA GSPYPAIARL TVAAPPSGGP GFLSIERPDS
     RPPRVGDTLN LNLRAVGSGA TFSHYYYMIL SRGQIVFMNR EPKRTVTSVS VFVDHHLAPS
     FYFVAFYYHG DHPVANSLRV DVQAGACEGK LELSVDGAKE YRNGESVKLH LETDSPALVA
     LGALDTALYA VGSKSHKPLN MGKVFEVMNS YDLGCGPGGG DSALQVFQAA GLAFSDGEQW
     TFSRKRLGCP KEKTTRRKRN VNFQKAINEK LGQYASPTAK RCCQDGVTRL PMRRSCEQRA
     ARVQQPDCRE PFLSCCQFAE SLRKKNRTRG QVGLQRALEI LQEEDLIDED DIPVRSFFPE
     NWLWRVETVD RFQILTLWLP DSLTTWEIHG LSLSKTKGLC VAAPVQLRVF RDFHLHLRLP
     MSVRRFEQLE LRPVLYNYLA RNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVAFS
     VVPTAAAAVS LKVVARGSFD FPVGDAVSKV LQIEKEGAIH TEELVYELNP LDHRGRTLEI
     PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV ASLLKLPQGC GEQTMIYLAP
     TLAASRYLDK TEQWSALPPE TKDHAVDLIQ KGYMRIQQFR KADGSYAAWL SRDSSTWLTA
     FVLKVLSLAQ EQVGGSPEKL QETSKWLLSQ QQADGSFQDP CPVLDRNMQG GLVGSDETVA
     LTAFVTIALH HGLAVFQDEG AEELKQRVEA SISKANSFLG EKASAGLLGA HAAAITAYAL
     TLTKASGDLR GVAHNNLMAM AQETGDNLYW GSVTSSQNNA VSPTPAPRNP ADPMPQAPAL
     WIETTAYALL HLLLHEGKAE MADQTAAWLT RQGSFQGGFR STQDTVIALD ALSAYWIASH
     TTEERGLNVT LSSTGRSGFR SHALQLNNRQ IRGLEEELQF SLGSKINVKV GGNSKGTLKV
     LRIYNVLDMK NTTCQDLQIE VTVKGHVEYT MEANEDYEDY EYDELPARDD PGVPLQPVTP
     LQLFEGRRNR RRREAPKLTS LSDRYVSHFE TEGPHVLLYF DSVPTSRECV GFEAVQEVPV
     GLVQPASAAL YDYYNPERRC SVFYGAPSKS RLLATLCSAE VCQCAEGKCP RQRRALERGL
     QDEDGYRMKF ACYYPRVEYG FQVKVLREDS RAAFRLFETK ITQVLHFTKD VKATVNQTRN
     FLVRASCRLR LEPGREYLIM GLDGATYDLE GHPQYLLDSN SWIEEMPSER QCRSTRQRAA
     CAQLHDFLQE YGTQGCQV
//
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