UniProt: A0A3Q1IN30

Database: UniProt
Entry: A0A3Q1IN30_ANATE

LinkDB:  A0A3Q1IN30_ANATE 
Original site:  A0A3Q1IN30_ANATE

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Ontology (3)   
   GO (3)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (41)   
   InterPro (20)   
   Pfam (11)   
   PROSITE (4)   
   SMART (6)   
All databases (47)   

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ID   A0A3Q1IN30_ANATE        Unreviewed;      1639 AA.
AC   A0A3Q1IN30;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Complement component c3a, duplicate 5 {ECO:0008006|Google:ProtNLM};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000021770.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000021770.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   STRING; 64144.ENSATEP00000021770; -.
DR   Ensembl; ENSATET00000022132.2; ENSATEP00000021770.1; ENSATEG00000013812.2.
DR   GeneTree; ENSGT00940000154063; -.
DR   InParanoid; A0A3Q1IN30; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd00017; ANATO; 1.
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; 2.60.40.1930; -; 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; IPR041425; C3/4/5_MG1.
DR   InterPro; IPR048848; C3_CUB2.
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; 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; PF07703; A2M_BRD; 1.
DR   Pfam; PF07677; A2M_recep; 1.
DR   Pfam; PF01821; ANATO; 1.
DR   Pfam; PF21308; C3_CUB2; 1.
DR   Pfam; PF17790; 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   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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1639
FT                   /note="Complement component c3a, duplicate 5"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018640681"
FT   DOMAIN          665..700
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01178"
FT   DOMAIN          1488..1637
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
SQ   SEQUENCE   1639 AA;  184557 MW;  17687AB9C420F73F CRC64;
     MCRTRLWLLS SLAFFFSTSL AHGSDMKVMS APNVLRIGTT ENIFVECQDC ADENELRVEI
     SVMKYPTKSE QLANTFVNLN RMNKFQSFGQ IKIPDRDFYK DPSVNQYVFL QAKFPDVELE
     KVVLVSFQFG YIFIQTDKTL YIPNSKVHYR IFALTPDMQP VQRDNETQLD ASIVINIVTP
     EGVILPLDPV SVKSGVYSGD YQLGEIVSPG LWKVVAKFYS KPQISFSAEF EVKEYVLPSF
     EVKLMTKNSF FYVDSEELTI NIKATYLFGE EVDGSAFGVF GVMHEDQKRS FPGSLQRVPI
     VKGEGSITLK KEHITQAVQN ILDLVGTSLF VAVSVLTESG NEMAEAELRN IQIVTSPYTI
     HFKKTPKYFK PGMSFDLAIE VVNPDGTPAQ GVVVVMNVDN VQGITAANGM ARLSINTVND
     PAPLKITATT SDPNISPERQ ASASMTALPY KSNNNNYMHI GVDMPEVTIG DNLKINLNLV
     RQENTENDIT YLILSRGRLV KFGNYRMKGQ LLISMIVPIT KHMLPSFRII AYYHTTQNEV
     VSDSIWVDVK DSCMGSLKLE SKSRSTLYEP RKMFELKITG DPEATVGLVA VDKGVYILNN
     KHRLSQKKIW DAVENYDTGC TPGGGKDSMS VFYDAGLVFE SNTCHFTLLL LVALSQYEDE
     VQRDCCLDGM RDTPVAYDCE RRSEYILDGA ACIEAFLHCC KEMKTQRAEK REGKLQLARS
     EEDDNSYMDS NEIVSRTKFP ESWLWSEIKL PACTKYNCDS TMLIRNVPLQ DSITTWQFTG
     ISLSRTMGIC VADPLEIIVR KEFFIDLRLP YSAVRGEQIE IKAILHNYQS DPATVRVDLT
     EMEHICSSAS KRGKYRQEVN VGAKATRSVP FVIIPTRDGQ YRIEVKASVK DSSLSDGIVK
     MLLVVPEGLL IKSPQIVTLD PEKKGVDGKQ VETINSRIPK KDLLPNTPTS TQISVTGTEY
     ALELKNEIAG PSMVDLVYQP SGCGEENMIH MTRFVITTTY LDKANKWEPV HIRKRSEALR
     HIYTGYQNQL NYRKKDGSFA AGSTHQSSTW LTAYVVKVFA MANSLVPVQS EVICDAVTFL
     IHNAQQPNGM FGELGGVSYR EMTGDVFGTD SDASMTAFCL IAMEESHTLC AATVDRLPES
     IDKARSYLRK RLSTLINPYA IAMASYALAS ENNLNQEILY KFASPDLSHW PVPGGRAYTL
     EATAYTLLAL VKAKAFKEAR HVVRWFNKQQ RAMDEGYGST QATLIVYQAV AAYWSSAKGP
     EYDLNVDILL PGRSKAVKYN FNSNNPYATR TSKASDINQD VTVTATGKGE ATLTMVSLYY
     ALPIEKESDC LKFNMSVALI PEKIDEDEKI YKLKIKVLYK DEERDATMSV LDIGFLTGFT
     INTKDLDLLS KGRARTIAKY KMNTIESERG SLIIYLDKVS HRRPEEISFR IHQKLKVGVL
     QPAAVSVYEY NNHEQKTDCV KFYHPERRAG ELLQLCRNDE CTCAEENCSM QKKGKINNDE
     RTDKACETEV NSRIDFVYKV HIEEFTDGLS TDIYSVRVLE AIKEGSLDVG PQGKLRTFLS
     YPHCRVALDL STGKTYLIMG RSKDVYPDDQ SQTYRYVLGE RTWIEYWPTD TECQTQKHNV
     TCSGIEEMVQ KYTLYGCRN
//

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