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Database: UniProt
Entry: A0A1S3QVV1_SALSA
LinkDB: A0A1S3QVV1_SALSA
Original site: A0A1S3QVV1_SALSA 
ID   A0A1S3QVV1_SALSA        Unreviewed;      1369 AA.
AC   A0A1S3QVV1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Complement C3-like {ECO:0000313|RefSeq:XP_014044031.1};
GN   Name=LOC106597357 {ECO:0000313|RefSeq:XP_014044031.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014044031.1};
RN   [1] {ECO:0000313|RefSeq:XP_014044031.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014044031.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   RefSeq; XP_014044031.1; XM_014188556.1.
DR   STRING; 8030.ENSSSAP00000069397; -.
DR   PaxDb; 8030-ENSSSAP00000069397; -.
DR   KEGG; sasa:106597357; -.
DR   OrthoDB; 4033541at2759; -.
DR   Proteomes; UP000087266; 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   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.20.210.20; -; 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; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
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; 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; PF07678; TED_complement; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SMART; SM00104; ANATO; 1.
DR   SMART; SM01419; Thiol-ester_cl; 1.
DR   SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1369
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010356782"
FT   DOMAIN          693..728
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01178"
FT   REGION          952..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1369
FT                   /evidence="ECO:0000313|RefSeq:XP_014044031.1"
SQ   SEQUENCE   1369 AA;  150998 MW;  AC021F2D9FABEA70 CRC64;
     MWVGNLLCLA ALAVALSLPT LSDGAALLVL SAPNLLRVGS NENIFVESQD HAGGPLNVKI
     MVKNHPTQSK ELASKSVVLD QANNFQAMTQ LVIPEGDHFV DDPKQKQYVV LQAQFPDRLL
     EKVVLVSFQS GYIFIQTDKT IYTPASTVYY RVFSMSPGLE PLTREIFVDK EVAKNKEIAV
     SVEIMTPENI TIFREIVNPD KGVKSGQFNL PEIVSFGTWH VVTRFQSTPQ KTFSSDFEVK
     EYVLPSFEVS LTPAKAFFYV DDKDLTVDIT ARYLYGKEVT GTGYVVFGVI TTENEKKSFP
     ASLQRVEIKE GKGVACLKKE HITQTFPNIN DLVKQSIFIS VSVLTEGGGE MVEAEKRGIQ
     IVTSPYTILF KRTPKYFKPG MPFDVSVYIT NPDNSPASGV EIDVTPDNAK GVTRDNGFAK
     ISLNTVASAK ELAITVKTKD PAIPDNRQAE ATMKALPYRT STGNFLHVGV DSNELKIGDP
     IKINLNLGPT PIQIHDLTYM FLSRGQLVKV GRFKRQGNAL VTLSVPVSKE MLPSFRIVAY
     YHVGADDLVA DSVWVDIKVS CMGSLKVTST RPKASYEPRK AFSLTVTGDP GAKVGLVAVD
     KGVYILNSKH RLTQAKIWDT IEKHDTGCTA GGGADNMGVF YDAGLVFETN TAKGTGIRTD
     PSCPVSSRRR RAVTISDVIT SMASKYNGLA KECCVDGMRD NTMGYTCDRR AQYITDGDVC
     IQAFLVCCTE MASKKTESKQ DALLLSRSEE DDDDEYMRSE DIVSRSQFPE SWMWEDTTLP
     ECPDQDKHCD STSVIRNNFL KDSITTWQIT AISLSKTHGI CVADPFEMIV LKEFFIDLKL
     PYSAVRNEQL EVKAILHNYS EDPITVRVEL MENGEVCSSA SKKGKYRQEV NMDAMSTRVV
     PYVIIPMKLG MHSIEVKASV KNSGSNDGVK RDLRVVAEGV LVKKETNVLL NPAKHGGEQT
     SHIPSGVPRN QVPNSEADTL ISVTGGEQTS VLVEQAISGD SLGSLIVQPV GCGEQNMIYM
     TLPVIATHYL DNTKKWEDIG LDKRNTAIKY INIGYQRELA YRKEDGSYAA WVQRQSSTWL
     TAYVVKVFAM SSTLISVQEN VLCSAVKWLI LNTQQPDGIF NEFAPVIHAE MTGNVRGSDN
     DASMTAFVLI AMQEASLLCE QSVNSLPGSM VKAVAYLEKR LPHLTNPYAV AMTSYALANA
     EKLNKETLLK FASPQLDHWP VPGGHQYTLE ATSYALLALV KVKAFEEAGP VVRWLNKQKK
     VGGGYGSTQS TIMVFQAVAE YWSHVKDLKD FDLDINLEVA GRASVTKWSI NNKNQFHTRT
     DKVKSIDKDL TVKASGNGEA TLSVVTLYYA LPEEKDSDCE SFDLSVTLT
//
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