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Database: UniProt
Entry: F1RT90_PIG
LinkDB: F1RT90_PIG
Original site: F1RT90_PIG 
ID   F1RT90_PIG              Unreviewed;       359 AA.
AC   F1RT90;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 5.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Aspartate beta-hydroxylase {ECO:0000313|Ensembl:ENSSSCP00000006641.5};
GN   Name=ASPH {ECO:0000313|Ensembl:ENSSSCP00000006641.5,
GN   ECO:0000313|VGNC:VGNC:85584};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000006641.5, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000006641.5, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000006641.5,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000006641.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; F1RT90; -.
DR   PeptideAtlas; F1RT90; -.
DR   Ensembl; ENSSSCT00000006826.5; ENSSSCP00000006641.5; ENSSSCG00000025087.4.
DR   VGNC; VGNC:85584; ASPH.
DR   GeneTree; ENSGT00940000156304; -.
DR   HOGENOM; CLU_023717_0_0_1; -.
DR   TreeFam; TF312799; -.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Bgee; ENSSSCG00000025087; Expressed in omentum and 44 other cell types or tissues.
DR   ExpressionAtlas; F1RT90; baseline and differential.
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; ASPARTYL/ASPARAGINYL BETA-HYDROXYLASE; 1.
DR   PANTHER; PTHR12366:SF33; ASPARTYL_ASPARAGINYL BETA-HYDROXYLASE; 1.
DR   Pfam; PF05279; Asp-B-Hydro_N; 1.
PE   1: Evidence at protein 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   Proteomics identification {ECO:0007829|PeptideAtlas:F1RT90};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        59..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..128
FT                   /note="Aspartyl beta-hydroxylase/Triadin"
FT                   /evidence="ECO:0000259|Pfam:PF05279"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  39406 MW;  E7973152F5959576 CRC64;
     MMAPRKNAKG GGGGNSSSSS SSSPSSCTSG GSSSPGARRE TKHGGQKNGK KGGLSGSSFF
     TWFMVIALLG VWTSVAVVWF DLVDYEEVLA KAKDFRYNLS EVLQGKLGIY DADGDGDFDV
     DDAKVLLGLK ERSAPKPTIP PEEAEPYPWL EDQVLEGPGP QNIEDELQDQ IQSLLDETVY
     PEHGEDLQQE QDAPAGELQL EDALLTGRDE DERIESMGTE AIHEETEDSY HVEETASPAY
     NQDTEDMMYE QENPESSEPV VEDDGRIYQE ADDVTYQDYD EQAVYEPAEN EGTESSDNAV
     DDSHTILEEV HVPPAEEQQE VPPETKRKTD DPEKKEKGDS FVFSDSVLSL ADSFLPSVC
//
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