ID V9K8V1_CALMI Unreviewed; 954 AA.
AC V9K8V1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Eosinophil peroxidase-like protein {ECO:0000313|EMBL:AFO94257.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94257.1};
RN [1] {ECO:0000313|EMBL:AFO94257.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFO94257.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; JW861740; AFO94257.1; -; mRNA.
DR AlphaFoldDB; V9K8V1; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR11475:SF63; EOSINOPHIL PEROXIDASE; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF00084; Sushi; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SMART; SM00032; CCP; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF49842; TNF-like; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000313|EMBL:AFO94257.1}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..954
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004777577"
FT DOMAIN 716..789
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 828..954
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 792..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491
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"
FT DISULFID 760..787
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 954 AA; 106626 MW; C36B08FECA4842B3 CRC64;
MTPVWLLGVM LIGFFQTLAE RVPPESERLL GTPFMKKAIQ EAIEWVDRSY KSTRENHREK
LRKQSLTPSD LLLFFKQPTA DTRRVVRAAE YTETALNLIQ KKVHQIHRRS LNATDLLSQA
DLDTIAKITG CAATRLTPKC EDDCWSNKYR TFSAECNNKN NPRLGSSNTP LARWLPPRYE
DGVSLPLGWT PGKLHSGFPL PLVREVSNSI LKIHNNEVIS DDTASHILVQ WGQWIDHDMT
LNPLSGSLET FNDGIRCENT CVQQSPCFPI KIPPNDTRIP DTNTCMPFYR SAPACGSGKL
GTLFGDVNTR EQINALTSFL DMSEVYGSTD CIANKLRNLS NELGLLAVNK EFTDKKLEHL
PFNTISTNLC GRQEESCAID KTKTPCFISG DVRVNEQLGL LAFHTLFLRE HNRLARELKK
LNPHWSGETV YQEARKIMGA FQEIIIYRDY IPRVIGEQEM EKHISNYNGY DETIDPRIAN
VFATAAFRFG HLSIQPTLFR FDENYQSDPT NGNLMLHKAF FTPWRAIKEG GIDPILRGMM
GNPAKRQIAG KMMPDELREN LFKLTSHLSL DLGSLNLQRS RDHGMPGYNA WRRFCGLSAP
RNVIELTQIV KSMDLAKKLL SLYGTPENID VWLGGISESF VQGGRVGPLF TCIIGKQFKK
LRDGDRFWWE NENVFTEPQK LALTSVSLSR IVCDNSNIKT LPPDAFNYAP NRQGHVTCDQ
LKRVDLSAWR EDVEVTPCGS VPVIAHGFFS LCMSSVRYTC ASGFQIAGGD TITCLGNGNW
DSAPPICKDD PEHVYGENSN DSTTSTGSSY GTGVVGPPGP KGDMGPPGLL KKSAFSAQLA
TDNVTPNTAI PFVTVIYNDN TGFNPATGIF TCQTAGVYSF SYNIEVHRRA SIILKKNGNT
IITSRIEDRS RANVMSGNII LSLAAEDKVW LEAPETGEMI HNLSFFMGFL IYTL
//
