ID G1Q8H4_MYOLU Unreviewed; 882 AA.
AC G1Q8H4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=NTR domain-containing protein {ECO:0000259|PROSITE:PS50189};
GN Name=LOC102422871 {ECO:0000313|Ensembl:ENSMLUP00000020007.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000020007.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000020007.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000020007.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: C3 plays a central role in the activation of the complement
CC system. Its processing by C3 convertase is the central reaction in both
CC classical and alternative complement pathways. After activation C3b can
CC bind covalently, via its reactive thioester, to cell surface
CC carbohydrates or immune aggregates. {ECO:0000256|ARBA:ARBA00002877}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AAPE02058281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1Q8H4; -.
DR STRING; 59463.ENSMLUP00000020007; -.
DR Ensembl; ENSMLUT00000031031.1; ENSMLUP00000020007.1; ENSMLUG00000023050.1.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000154063; -.
DR HOGENOM; CLU_001634_6_1_1; -.
DR InParanoid; G1Q8H4; -.
DR OMA; ISICARY; -.
DR TreeFam; TF352568; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR CDD; cd02896; complement_C3_C4_C5; 1.
DR CDD; cd03583; NTR_complement_C3; 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; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 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; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR049466; C3_CUB1.
DR InterPro; IPR048848; C3_CUB2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; COMPLEMENT C3; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF21406; C3_CUB1; 1.
DR Pfam; PF21308; C3_CUB2; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SFLD; SFLDG01179; Complement_C3/C4_Like; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS50189; NTR; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Complement alternate pathway {ECO:0000256|ARBA:ARBA00023162};
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunity {ECO:0000256|ARBA:ARBA00023162};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00023162};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT DOMAIN 737..880
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 882 AA; 99561 MW; 30B1E624CA10DE2C CRC64;
PPRISSKTIK VFLRDSITTW EIMAVSLSDR KAGICVADPY EVTVVQDFFI DLRLPYSVVR
NEQVEIRAVL YNYREEDTLT VRVEMLYNPA FCSLATAKKR HLQTVYIPPK SSLAVPYVIV
PLKTGLQEVE VKATVYRYFI TDGVRKTLKV VPEGIRMNKT VAVKTLDPQH LGQNGVQRVE
VEAADLSDQV PDTESETRIL LQGTPVAQMA EEAIDGERLK HLIVTPSGCG EQNMIGVTPT
VIAVHYLDHT EQWDKFGIDK RQEALDLIKK GYTQQLAFRQ PNKAFAAFLN MKSSTWLTAY
VVKVFSLAAN LIAIDSEVIC GAVKWLILEK QRPDGVFQED GPVIHQEMIG GYREAEEKDV
SLTAFVLIAL QEAKDICEGQ VNSLGGSINK AGDFLEAHYM NLKRPYAVAI AGYALAQLGK
LEDPLLNTFL NAATDKNRWE EPGKRLYSVE ATSYALLALL LLKDFDSIPP VVRWLNEQRY
YGGGYGSTQA TFMVFQALAQ YQRDVPDHED LNLDVSIDLP SRSSAVTHRI LWESASLLRS
ETTKENEDFT LTAKGKGQGT LSVVTMYQAK IKGGAPCKKF SLRVNIQPAP EAKKPQDAKN
TMLLNICTRY LGDQDATMSI LDISMMTGFA PDPADLKQLA SGTDRYISKF ELDNKAFSNK
NTLIIYLNKI SHDQEDCIAF KVHQYFNVGL IQPGAVKVYS YYNLDESCTR FYHPEKEDGL
LSKICHNEIC RCAEESCFMH QSDDQVTPDD RLDKACEPGV DYVYKTLLLR KELSDDFDEY
IMVIKLIIKS GTDEVQPEQE RRFISHVKCR AALKMQEGKH YLIWGLSSDL WGEKSNIKYI
IGKDTWVELW PEADECQDDE NKKLCRDLAS FRENMIVFGC PN
//
