Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Complement C3

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-GGA-2132273. Formation of membrane-bound convertase C3.
R-GGA-2132281. Regulation of complement cascades.
R-GGA-2132285. Complement Cascade.
R-GGA-2132293. Formation of fluid-phase convertase C3.
R-GGA-2173345. Anaphylatoxins initiate inflammatory responses.

Names & Taxonomyi

Protein namesi
Submitted name:
Complement C3Imported
OrganismiGallus gallus (Chicken)Imported
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus

Subcellular locationi

  • Secreted SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

SecretedSAAS annotation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 16521635Sequence analysisPRO_5004318644Add
BLAST

Keywords - PTMi

Disulfide bondSAAS annotation

Proteomic databases

PaxDbiQ90633.
PRIDEiQ90633.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000018740.

Structurei

3D structure databases

ProteinModelPortaliQ90633.
SMRiQ90633. Positions 743-928, 988-1287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini686 – 72136Anaphylatoxin-likeInterPro annotationAdd
BLAST
Domaini1506 – 1650145NTRInterPro annotationAdd
BLAST

Sequence similaritiesi

Contains NTR domain.SAAS annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOVERGENiHBG005110.
KOiK03990.
PhylomeDBiQ90633.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q90633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLLLPLLL GVLLLHAVPT PAQMVTMVTP AVLRLDTDEK VVLEAPGLSA
60 70 80 90 100
PTEANILVQD FPQKRKVLFQ VRKQLNPAEG MMAIATVKVP VKLLPPVVGK
110 120 130 140 150
HFVSVVARVG QVTLEKVLLV SLQSGHIFLQ TDKPIYTPGS TVLSRLFALS
160 170 180 190 200
HFMQPLLKTV IVEVKTPDNV IIKQVPVSSP MRNGIFSINH NLPEVVSLGT
210 220 230 240 250
WTITAKFEDS QDQVFSTQFE VKEYVLPSFE VTLDPQEKFL YIDPAEDFRV
260 270 280 290 300
TITARYLYGK NLQGTAFVLF GVVVDDEKKT IPQSLQRVKV TDGDGQAVLP
310 320 330 340 350
MAMLRQPFAN LQELVGHSLY VTVTVLTESG SDMVEAQRSG IRIVTSPYTI
360 370 380 390 400
HFTHTPKYFK PGMPFDPTVY VTNPDNSPAA AGIPVKADNF QGLVSTQRDG
410 420 430 440 450
TAKLVLNMPA NKNSVPITVR TDQKDLPPER QASRQIVAEA YQSQGNSGNY
460 470 480 490 500
LHLAVGASQV QPGDNLPINF HLKSNRDDVR KSVSYFTYLI LSKGHIVHVG
510 520 530 540 550
RQPREGDQSL VTMSLPVTAN LIPSFRIVAY YHVKPGEIIA DSVWVDVKDT
560 570 580 590 600
CMGSLVVRGA SEADNRVHEP RTPMRLHIEG DHKAHVGLVA VDKAVYVLNK
610 620 630 640 650
NKLTQSKVWD TVENSDIGCT PGSGRNQVGV FADAGLSLTS NVNINTEQRS
660 670 680 690 700
EVQCAKPAKR KRRSVRLIKH KGTKMAEYSD KNLRKCCEDG IRKNLMGYSC
710 720 730 740 750
EKRATYVLDA KSCTEAFLSC CLYIKGIRDE ERELQYELAR SEVDDAFLSD
760 770 780 790 800
EDITSRSLFP ESWLWQVEEL TEPPNEQGIS MKTLPIYLKD SITTWEVLAV
810 820 830 840 850
SISENKGLCV ADPYEITVMK EFFIDLRLPY SAVRNEQVEV RAILYNYWTN
860 870 880 890 900
KIKVRVELMY NPALCSASTT KTRYQQIFQL EPQSSDAVPF VIVPLELGQH
910 920 930 940 950
DVEVKAAVWN SFVSDGVKKK LRVVPEGMRL EKTVKIVELD PKTLGNNGVQ
960 970 980 990 1000
EVKVKAANLS DIVPNTESET KVSIQGNPVS ILVEKATDGT KLKHLIVTPS
1010 1020 1030 1040 1050
GCGEQNMIGM TPTVIAVHYL DSTMQWETFG INRRTEAIEL IKKGYTQQLA
1060 1070 1080 1090 1100
YRKEDGSFAA FTTRPSSTWL TAYVAKVFAM AINMVDIKPE VVCGAIKWLI
1110 1120 1130 1140 1150
LEKQQPDGLF QEDAPVIHKE MVGGYHGAEP SVSLTAFVLS ALQESQKICK
1160 1170 1180 1190 1200
NYVKSLDGSI AKASDYLSRK YQSLTRPYTV ALTSYALALT GKLNSEKVLM
1210 1220 1230 1240 1250
KFSKDGTHWA ERNAHTYNIE GTSYALVALL QMEKAELTGP VVRWLAQQNY
1260 1270 1280 1290 1300
FGGGYGSTQA TILVFQALAQ YHVALPRHVE LNLDVSVLLP RRANAITYRI
1310 1320 1330 1340 1350
ENNNALVARS AETKLNEDFT VKAEGTGKGT MTVVTVYKAK VPEKENKCDN
1360 1370 1380 1390 1400
FDLRVSVEDV KAGREVEGVI RSVKITICTR FLDTVDATMS ILDISMLTAF
1410 1420 1430 1440 1450
SPDVQDLKSL SEGVERYISK FEIDHALSNR SNLIIYLDKV SHQVEECIAF
1460 1470 1480 1490 1500
RAHQHFQVGL IQPASVIVYS YYKIDDRCTR FYHPDKAGGQ LRKICHGEVC
1510 1520 1530 1540 1550
CAEENCFIRV KKDNPITVNE RIDLACKPGV DYVYKVKVVA TEETPSHDNY
1560 1570 1580 1590 1600
IMSILTVIKM GTDENPGGSN RTFVSHKQCR DALSLQKGQD YLVWGLASDL
1610 1620 1630 1640 1650
WVTGSRFSYL ISKDTWLEAW PLEESCQDAD LQPLCQDFTE FSDNLVLFGC

PT
Length:1,652
Mass (Da):184,086
Last modified:November 1, 1996 - v1
Checksum:i9020C49FE127BD1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16848 mRNA. Translation: AAA64694.1.
PIRiI50711.
RefSeqiNP_990736.1. NM_205405.1.
UniGeneiGga.48596.

Genome annotation databases

GeneIDi396370.
KEGGigga:396370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16848 mRNA. Translation: AAA64694.1.
PIRiI50711.
RefSeqiNP_990736.1. NM_205405.1.
UniGeneiGga.48596.

3D structure databases

ProteinModelPortaliQ90633.
SMRiQ90633. Positions 743-928, 988-1287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000018740.

Proteomic databases

PaxDbiQ90633.
PRIDEiQ90633.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396370.
KEGGigga:396370.

Organism-specific databases

CTDi718.

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
HOVERGENiHBG005110.
KOiK03990.
PhylomeDBiQ90633.

Enzyme and pathway databases

ReactomeiR-GGA-2132273. Formation of membrane-bound convertase C3.
R-GGA-2132281. Regulation of complement cascades.
R-GGA-2132285. Complement Cascade.
R-GGA-2132293. Formation of fluid-phase convertase C3.
R-GGA-2173345. Anaphylatoxins initiate inflammatory responses.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ90633_CHICK
AccessioniPrimary (citable) accession number: Q90633
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.