ID A0A2R9AYC7_PANPA Unreviewed; 1725 AA.
AC A0A2R9AYC7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPAP00000020054.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000020054.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000020054.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000020054.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AJFE02111595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9597.ENSPPAP00000020054; -.
DR Ensembl; ENSPPAT00000042839.1; ENSPPAP00000020054.1; ENSPPAG00000032907.1.
DR GeneTree; ENSGT00940000155739; -.
DR Proteomes; UP000240080; Chromosome 6.
DR Bgee; ENSPPAG00000032907; Expressed in liver and 6 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:Ensembl.
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; -; 1.
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); 2.
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:UP000240080};
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..1725
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015331712"
FT DOMAIN 683..717
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1576..1723
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 1725 AA; 190669 MW; 324C4B4D8319944B CRC64;
MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVVKGS VFLRNPSHNN
VPCSPKVDFT LSSERDFALL SLQVPLKDAK RCGLHQLLRG PEVQLVAHSP WLKDSLSRTT
NIQGINLLFS SRRGHLFLQT DQPIYNPGQR VRYRVFALDQ KMRPSTDTIT VTVENSHGLR
VRKKEVYMPS PGTWKISARF SDGLESNSST QFEVKKYVLP NFEVKITPGK PYILTVPGHL
DEMQLDIQAR YIYGKPVQGV AYVRFGLLDE DGKKTFFRGL ESQTKLVNGQ SHISLSKAEF
QDALEKLNMG ITDLQGLRLY VAAAIIESPG GEMEEAELTS WYFVSSPFSL DLSKTKRHLV
PGAPFLLQAL VREMSGSPAS GIPVKVSATV SSPGSVPEVQ DIQQNTDGSG QVSISIIMPQ
TVSELQLSVS AGSPHPAIAR LTVAAPPSGG PGFLSIERPD SRPPRVGDTL NLNLRAVGSG
ATFSHYYYMI LSRGQIVFMN REPKRTLTSV SVFVDHHLAP SFYFVAFYYH GDHPVANSLR
VDVQAGACEG KLELSVDGAK QYRNGESVKL HLETDSLALV ALGALDTALY AAGSKSHKPL
NMGKVFEAMN SYDLGCGPGG GDSALQVFQA AGLAFSDGDQ WTLSRKRLSC PKEKTTRKKR
NVNFQKAINE KLGQYASPTA KRCCQDGVTR LPMMRSCEQR AARVQQPDCR EPFLSCCQFA
ESLRKKSRDK GQAGLQRALE ILQEEDLIDE DDIPVRSFFP ENWLWRVETV DRFQILTLWL
PDSLTTWEIH GLSLSKTKGL CVATPVQLRV FREFHLHLRL PMSVRRFEQL ELRPVLYNYL
DKNLTVSVHV SPVEGLCLAG GGGLAQQVLV PAGSARPVAF SVVPTAAAAV SLKVVARGSF
EFPVGDAVSK VLQIEKEGAI HTEELVYELN PLDHRGRTLE IPGNSDPNMI PDGDFNSYVR
VTASDPLDTL GSEGALSPGG VASLLRLPRG CGEQTMIYLA PTLAASRYLD KTEQWSTLPP
ETKDHAVDLI QKGYMRIQQF RKADGSYAAW LSRDSSTWLT AFVLKVLSLA QEQVGGSPEK
LQETSNWLLS QQQADGSFQD LCPVLDRSMQ GGLVGNDETV ALTAFVTIAL HHGLAVFQDE
GAEPLKQRVE ASISKANSFL GEKASAGHLG AHAAAITAYA LTLTKAPADL RGVAHNNLMA
MAQETGDNLY WGSVTGSQSN AVSPTPAPRN PSDPMPQAPA LWIETTAYAL LHLLLHEGKA
EMADQAAAWL TRQGSFQGGF RSTQDTVIAL DALSAYWIAS HTTEERGLNV TLSSTGRNGF
KSHALQLNNR QIRGLEEELQ FSLGSKINVK VGGNSKGTLK VLRTYNVLDM KNTTCQDLQI
EVTVKGHVEY TMEANEDYED YEYDELPAKD DPDAPLQPVT PLQLFEGRRN RRRREAPKVV
EEQESRVHYT VCIWRNGKVG LSGMAIADVT LLSGFHALRA DLEKLTSLSD RYVSHFETEG
PHVLLYFDSV PTSRECVGFE AVQEVPVGLV QPASATLYDY YNPERRCSVF YGAPSKSRLL
ATLCSAEVCQ CAEGKCPRQR RALERGLQDE DGYRMKFACY YPRVEYGFQV KVLREDSRAA
FRLFETKITQ VLHFTKDVKA TANQMRNFLV RASCRLRLEP GKEYLIMGLD GATYDLEGHP
QYLLDSNSWI EEMPSERLCR STRQRAACAQ LNDFLQEYGT QGCQV
//