ID A0A3B3ZT71_9GOBI Unreviewed; 1420 AA.
AC A0A3B3ZT71;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000007501.1};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000007501.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000007501.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 409849.ENSPMGP00000007501; -.
DR Ensembl; ENSPMGT00000007981.1; ENSPMGP00000007501.1; ENSPMGG00000006220.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09826; peroxidasin_like; 1.
DR Gene3D; 6.20.200.20; -; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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 InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF75; PEROXIDASIN HOMOLOG; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01463; LRRCT; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017436298"
FT DOMAIN 195..283
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 291..377
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 382..467
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 474..559
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1354..1412
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT COILED 1330..1357
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1023
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 1420 AA; 158929 MW; 64F437627F39C8FB CRC64;
MALRAGHFSF APRCLLAVAV LLLAGGPQLA RSCPSRCLCF RTTVRCMHLN LETVPAVSPQ
TTILLLNNNH IRRIPRGAFE DLENLKYLYL HFNNIESLEP ESFAHLPKLE RLFLHNNRIT
QLVPGTFSHL QAMKRLRLDS NALNCDCELL WLADLLKQYA ESGNAQAAAT CDYPSRLQGR
SVATLTAEEL NCEVPRITSE PQDVDVTSGN TVYFTCRAEG NPKPQIIWLR NNNALNMRED
HRLNLLEDGT LMIQDTRETD QGVYQCMAKN VAGEVKTSQV TLRYFGAPSR PSFVIQPQNT
EVLVGESVTL ECSATGQPQP RVTWTKGDRT PIPSDTRINI TPSGGLFIQN VVQADGGQYT
CFASNNVDTI HATAYIIVQA IPQFSVTPQD QSVLEGHTVD FPCEATGYPQ PVVAWTRGGS
PLPIDRRHTV LSTGTLRITR VAAHDEGQYE CQAVSPVGTV RTAVQLSIQQ RVTPVFTNAP
RDLTVESGQD VQIPCSAQGQ PQPVLTWNKD GVQVTESGKF HISLDGYLEV KDVGTADAGR
YECIARNSIG YQVASMVLTV IVPPVSREGD TFVSTSIQQA IRNVDSAIES TRRRLFDGQP
RTPGEILALF RYPRDPYTVE QARAGEIFEQ TLLLIQNHVN QGLMVDTNGT AFRYNDLVSP
RFLDMIANLS GCTAHRRLNN CSDICFHQKY RSHDGTCNNL QHPMWGASLT AFERLLKPVY
DNGFNLPRGA MERPHNGYRL PLPRLVSTTM IGTETITPDD RYTHMLMQWG QFLDHDLDAT
VASLSQSRFS DGQLCAQVCT NDPPCFPIQF PPNDPRQIRS GARCMFFVRS SPVCGSGMTS
LLMNSVYPRE QTNQLTSYID ASNVYGNSRH ESEEVRDLAS HRGLLRQGII QRTGKPLLPF
ATGPPTECMR DENESPIPCF LAGDHRANEQ LGLTAMHTVW FREHNRIATE LLRLNPHWDG
DTIYHEARKI VGAQMQHITY NHWLPKIFGE AGMRMMGQYT GYNPNINAGI FSAFATAAFR
FGHTLINPIL YRLDEDFQPI PQGHLSLHRA FFSPFRIVNE GGIDPLLRGL FGVAGKMRVT
TQLLNTELTE KLFSMAHAVA LDLAAMNIQR GRDHGISPYN DFRTFCNLSS AQTFEDLRNE
IKNPTVREKL QRLYGTPLNI DLFPALMAED LVPGSRLGPT LMCLLVTQFK RVRDGDRFWY
ENPGVFTPAQ LTQLKQASLA RVLCDNGDNI TRVQQDVFSV AELPHGFGSC EDIPHIDLRM
WQDCCEDCRT KGQFNALSYH FRGRRSAEHS YNEDKPVDSP VGSSLESAEN VTAKAQKTTQ
PTVTDFQDFV SEMQKTITSL RKQIKRLEAR LRRTDCTDSE GRERADGEQW KQDPCTTCEC
TDAQVTCTVQ SCPPAQCKHP VKLKGACCPM CLQQENNRHI
//
