ID A8XR70_CAEBR Unreviewed; 1366 AA.
AC A8XR70;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Protein CBR-PXN-2 {ECO:0000313|EMBL:CAP35167.2};
GN Name=pxn-2 {ECO:0000313|WormBase:CBG17537};
GN Synonyms=Cbr-pxn-2 {ECO:0000313|EMBL:CAP35167.2};
GN ORFNames=CBG17537 {ECO:0000313|WormBase:CBG17537}, CBG_17537
GN {ECO:0000313|EMBL:CAP35167.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP35167.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP35167.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP35167.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-
CC [protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000256|ARBA:ARBA00033700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357;
CC Evidence={ECO:0000256|ARBA:ARBA00033700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O;
CC Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:166867; Evidence={ECO:0000256|ARBA:ARBA00033691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021;
CC Evidence={ECO:0000256|ARBA:ARBA00033691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-
CC tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000256|ARBA:ARBA00033621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361;
CC Evidence={ECO:0000256|ARBA:ARBA00033621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29250; Evidence={ECO:0000256|ARBA:ARBA00033705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017;
CC Evidence={ECO:0000256|ARBA:ARBA00033705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O;
CC Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:166867;
CC Evidence={ECO:0000256|ARBA:ARBA00033612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025;
CC Evidence={ECO:0000256|ARBA:ARBA00033612};
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DR EMBL; HE600959; CAP35167.2; -; Genomic_DNA.
DR STRING; 6238.A8XR70; -.
DR WormBase; CBG17537; CBP41915; WBGene00037136; Cbr-pxn-2.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_006087_0_0_1; -.
DR InParanoid; A8XR70; -.
DR OMA; QHFKCAK; -.
DR OrthoDB; 4560at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:EnsemblMetazoa.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IEA:EnsemblMetazoa.
DR GO; GO:0071711; P:basement membrane organization; IEA:EnsemblMetazoa.
DR GO; GO:0010172; P:embryonic body morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0016203; P:muscle attachment; IEA:EnsemblMetazoa.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:EnsemblMetazoa.
DR GO; GO:0110011; P:regulation of basement membrane organization; IEA:EnsemblMetazoa.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09826; peroxidasin_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF141; PEROXIDASIN HOMOLOG PXN-2; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1366
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002730883"
FT DOMAIN 365..457
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 464..551
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1323
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1045
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1366 AA; 155249 MW; 98E0EAD82D2BF323 CRC64;
MRLASLILVL LPFTIACPSE CQCSGLDVHC EGKSLTTIPS HIPIATTNLY FSNNLLSSLR
KSDFHSLPNL QYLDVSNNTI RTVEETVIDG FPGLKYLDLS WNKVKIVPKL STSPNALVSL
NLAHNDISKL DDDVSFTFLL SRNLIYLMSN SPYLQTFSLQ RNRVQTLSHD FFTNRMVPTL
KTVKMAGNPW SCDCRLIQLK TMANALLAYS NRNTFVIGKC FFPKDLRNQV FKNLELEDFK
CTKPEFSKTD DGMFKMSCPN NEMEPYHYDS VFLENNKEAR HTAHFARDKD GSLLSNGPFT
RNYQCAFHRQ KQSIHSLKKA QAGTTESTTM ETSTTMETTT TMETTTTTME QMTTTEKMLV
TTEMPEADHQ SMFIHRQADT SSRDGETSEL MCEAEGDPMP VMSWMFGNEK LVESRKHKFS
KNGSVLKIFP FLNTDVGQYK CIATNDEESE AHMFTVSLKE RQQPVIVDAP MNTNATIGQQ
VTFRCNAKGF PTPDVVWLFE GTRIPRRNTR YTISDNNIEL TIEKVTRHDS GVFTCQAVNS
VGSAVATANL LVGAELTEKV DKLLDDSTIE KIAKEAKQKV ENALASTKDQ RKMDKIESPH
DLRKLFKFAI NLKKVDLGKA REIYEESIRL VQMHIDNGLA FEAKMISPNV SYEAVLPVSY
VQTLMEKSGC QTGQFAESCE DYCFFSKYRS YDGQCNNQEN PWWGVSEMAF LRLLPPRYEN
GFNTPVGWEK GKMYNGYQVP NARKVSRVLI GTDETTPHSH LSAMTMQWGQ FIDHDLTLTA
PALTRHSYKE GAFCNRTCEN ADPCFNIQLE ADDPKLHTGL YQKHPCMEFE RNGAACGSGE
TSPIFQRVTY RDQLNLLTSY LDASGIYGNS EEQALELRDL YSDHGLLRFD IVSSANKPYM
PFEKDSDMDC RRNYSRENPI KCFLAGDIRA NEQVGGGGDV IAGGHKIFFL QLGLMSMHTI
FLREHNRIAS KLLEVNENWD GETIFQETRK IIGAMLQHIT YNDWLPKILG KATYDTIIGE
YKGYNPETNP TIANEFATAA LRFAHTLINT HLFRFDKDFK ETKEGHLPLH NAFFAPERLV
SEGGVDPLLR GLFAAPIKLP RPDQVLNKEL TEKLFNRYHE VALDLAALNI QRGRDHGLPT
WTEYRKFCNL TVPKTWADMK NIVQNDTVIA KLQSLYGVPE NIDLWVGGVT EKRTADALMG
PTLACIIADQ FKRLRDGDRF WYENDEMFSK TQLRQIKKVT LSKIICTNGD DIDRIQRDIF
VYHGNSTQFY ESCDALPEIN LNMWTTCCDA MCSSSSSLAR NAIGGDEKAK RRKRRHHPKK
SCHDEGKKQK SGDRWSHAND ICIECMCDDG EVWCKTRDFC KQSDLK
//
