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Database: UniProt
Entry: U3JAJ7_DANRE
LinkDB: U3JAJ7_DANRE
Original site: U3JAJ7_DANRE 
ID   U3JAJ7_DANRE            Unreviewed;      2105 AA.
AC   U3JAJ7; A0A8M1NAL3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Si:dkey-61p9.11 {ECO:0000313|Ensembl:ENSDARP00000127265};
GN   Name=fasn2 {ECO:0000313|ZFIN:ZDB-GENE-041210-242};
GN   Synonyms=si:dkey-61p9.11 {ECO:0000313|RefSeq:NP_001041530.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000127265};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000127265, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000127265};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000127265}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000127265};
RG   Ensembl;
RL   Submitted (SEP-2013) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:NP_001041530.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001041530.1};
RX   PubMed=30974150;
RA   Thiessen K.D., Grzegorski S.J., Chin Y., Higuchi L.N., Wilkinson C.J.,
RA   Shavit J.A., Kramer K.L.;
RT   "Zebrafish otolith biomineralization requires polyketide synthase.";
RL   Mech. Dev. 157:1-9(2019).
RN   [4] {ECO:0000313|RefSeq:NP_001041530.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001041530.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
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DR   EMBL; AL935186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001041530.1; NM_001048065.1.
DR   STRING; 7955.ENSDARP00000127265; -.
DR   PaxDb; 7955-ENSDARP00000127265; -.
DR   Ensembl; ENSDART00000152922; ENSDARP00000127265; ENSDARG00000096762.
DR   Ensembl; ENSDART00000152922.2; ENSDARP00000127265.1; ENSDARG00000096762.2.
DR   GeneID; 100000781; -.
DR   KEGG; dre:100000781; -.
DR   AGR; ZFIN:ZDB-GENE-041210-242; -.
DR   ZFIN; ZDB-GENE-041210-242; fasn2.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_35_2_1; -.
DR   OMA; IINHCTG; -.
DR   OrthoDB; 5396558at2759; -.
DR   PhylomeDB; U3JAJ7; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000437; Alternate scaffold 4.
DR   Proteomes; UP000000437; Chromosome 4.
DR   Bgee; ENSDARG00000096762; Expressed in intestine and 6 other cell types or tissues.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..431
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2014..2089
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2105 AA;  233600 MW;  D8736E456B71C31D CRC64;
     MDDDTEIAIV GVGCHFPGGE GLENFWRVLL EGKNCAVQIP NDRFNLSQWY DPEESKAGKT
     YTAKAALIDG LNAFDHKFFG ITEAESLSMD PQHKLLLQCT YRALEDAGIP MEKASGTRTG
     VYLGLMNRDF ELATVRNNPK HISHTTGTGV AMSIAANRIS YIFNFTGPSV AIDCACSSSL
     VALHFACQAI KQGDCDMSVC GGVSCILEPA LFVALSKAKM ISPDGTSKPF SSKADGYGRG
     EGCGVVLLKP LKRALEDHDH IWGVIGKTAV NQDGHSVSPI TKPSMVQQEE LLRKIYSTEA
     DLCSVQYIEA HGTGTPVGDP VEAGSMSKVI AKERSQKSGP LIIGSVKSNI GHTESAAGVA
     GLIKVLLMMQ HETIVPSLFY SKENSSIDLK SLNMNIPTRV QKWISNNRAG RIAGINNFGF
     GGTNAHAIVK QYVQSKKPKS QPISKSCQYF VVSAASEKSM RNIIRDTADQ IGAGKISDLQ
     SLLYTSACRR SHLKHKYRNA FQTSSLADLQ DKLTAAVDKR LVLSKTDSRV VFVFCGNGVT
     YQGMCQQLLK HETVFREEIV KIETLLKIYR RQNLIEMLEG RSEMSKDLSD PQLVQPLLFA
     IQVAVFKLLK HWGISPDAVL GHSIGEVAAA HCSGLLSLED AVKVIHYRSS LQSTVTGGKM
     LVVSNMAVSE ILNMLPSHSG RVCLAAYNSP QSCTLSGDAA EIDSLHQKLS SSTNGKDLFL
     RILDVPAAYH SHMMDPIVSR VKEDIGSLQT CDLEMELFST VTGVSSCSTD FITGEYWARN
     IRQAVEFEQA VKSATKNKRN VIFVEIGPRR SLQRYITETL GKDIAVVPAV QPDKDHETML
     AVVSKLFELG ANINWDLFYK GWEAEPIPFP RYQFDDVKRE VFASDLQLTG TTRNHPVVTQ
     MSTDSSVFSC DLSSESVAFL QDHKHNGVAI IPGAFYTELG LATFMEYAKP KVPLSSLQLS
     ITFQSPLTFT QNAPHIKVQL ENLADSMHNF KIHSTSAVYA FGSVEVQPGR RPEEQFISLD
     SISRRCTLHM TSEEFYKQLS QTGFQYGSVF RNKADVYCGE EFREALSVVK VPKELLHQLH
     DYHLHPVVLD YFMQLAPVTL GNDQSARPQF PAQIASLTVF EPLQEELVVY LRAVDVGDDG
     FEICGCLANK QGRVLVEIKH VKIKMIGSRS EVVKEYFFHN SFDIISEDDM LDTQIKALVF
     SDQLGIFKAL QQHLDSRSRC VSFSDSSTLL EGGVETLLSK LAISSVKKNF QEILFMWSDA
     DLTTLESEKV LESMAGCCEM FRKTVRYLKA LQFPGVIRVI TYRSSESIVD SINPGYVLTG
     MTRACAAELQ ELSFQLIDMG SGTSEDIKAL VQVLRSYPCH KYPELVVKEG NILQPEITHT
     PLPSMASPLQ KVHMLDEELF ILQTSDPYAM RNLSATEMEN SIQPIQGKHV ELHLNKICVH
     SSDYFPVSMS DLSYGHTLYW NKHTSQHHNL LALDYSGTVT AVGKDVSKFK VGDHVVSCYP
     VSATSKVVIP AAVCCKAKRL SFLNDIPCVS YMVLAWEILH KALPKIKVQR KLGIFSTVPD
     SALINVLLAI ANRSGWNVKV CTQTDQLSCD FSEVVGAVFL PPYNLVTAEV ASRIKGINDI
     VFVCDNQTEV PLNSATFRST NEEVHFHFVF MSQVLQKWSL QTQMPKIYRW QKSMHLNRKS
     MSLDTTAVQR ANSQHIDLLS VKESDSYFTC QILPIIILNS EDKNQLSEIP VIPKNNLFKK
     KSVYIVTGGL TGLGFETVKF IAQKGGEHIV ILSRRNPNPE MQQEISQLSS RCGSVIKSLP
     CDVSVSEQVD QTIAKVKKLF PSSPIKGVFH SAVVLHDGLI ERLDKSLYEK VMRPKVNGVI
     NLHRATIQCN LDYFVCYSSI SAFMGNASQT NYAAANTFMD TFCQYRRNIG LAGQSINWGA
     LNLGLLLDKV HFQRFLEAKG ILLLEVPEIH ESLEQCLLIN KPQQVVCRFS FKNSWNSVLS
     QNKSLNARLF KIAKEAFIRA GVNPSRPEQP MTSSSPHDYL RFLISETAGV EKDELSDDVH
     LFELGIDSML AMTLQNHIFS YRGVNIPLVT LLDPNSTLST ITKILEENGV DEYQSASYES
     TSTYL
//
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