ID V9KD33_CALMI Unreviewed; 533 AA.
AC V9KD33;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aspartyl/asparaginyl beta-hydroxylase {ECO:0000313|EMBL:AFO95651.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO95651.1};
RN [1] {ECO:0000313|EMBL:AFO95651.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFO95651.1};
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).
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DR EMBL; JW863134; AFO95651.1; -; mRNA.
DR AlphaFoldDB; V9KD33; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0062101; F:peptidyl-aspartic acid 3-dioxygenase activity; IEA:InterPro.
DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR InterPro; IPR039038; ASPH.
DR PANTHER; PTHR12366:SF32; ASP-B-HYDRO_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12366; ASPARTYL/ASPARAGINYL BETA-HYDROXYLASE; 1.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..106
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 59515 MW; 2C7C86367B607B9A CRC64;
MGPKSKSKGS NPTSRRDKPT PLNKNGKKSD GPSGSSFFTW FMIIALLGVW TSVAVVWFDL
VDYEDVLAKA KEFRYNLSEV LQGKLGVYDA DGDGDFDMED AKVLLGLKER AAPAAPAGKT
EEPVHHSVNI PLETAETQAE DSEPEPEPLQ ASETHADLRS EPEEAVEEDE EEEEEELEPE
LAEETEEDVA AETDEVEHEE QEAESEVADI PPAEPEEVEE EPVTEHAEAA GESKDEVEEE
TLPEPAEILE DSEEEVSEVT DHDEAEIAES EVEEDEADNE GDLDGATLEP EEVVSEREES
LGDYEIEAES QTEKDDSDQV EEEEQDSDQV DADLYNQMAQ DFFDQGESEG ETEEEVVVSD
EYIEEYEAPV SEDATEEYYA EEPDYVPGNE DVQEALPVPE KTDKDSQRAA VPLPEPVEEV
TKEERDAPKT TEEHPAEEVT AEEHSEEHVY HAEELTDEEE HMDVVEVHTH VEEHTEGNEP
TEPDHSEDTG EVEETMTRDK TEPEEQLGDT DSQEEPAVET ISPSKIEDKP LDL
//
