ABD12_DANRE
ID ABD12_DANRE Reviewed; 382 AA.
AC Q08C93; B0R177;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lysophosphatidylserine lipase ABHD12 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8N2K0};
DE AltName: Full=2-arachidonoylglycerol hydrolase ABHD12 {ECO:0000305};
DE AltName: Full=Abhydrolase domain-containing protein 12 {ECO:0000305};
DE AltName: Full=Monoacylglycerol lipase ABHD12 {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:Q8N2K0};
DE AltName: Full=Oxidized phosphatidylserine lipase ABHD12 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8N2K0};
GN Name=abhd12 {ECO:0000250|UniProtKB:Q8N2K0};
GN ORFNames=si:ch211-79l10.2, zgc:153367 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 93-371.
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27890673; DOI=10.1016/j.nbd.2016.11.008;
RA Tingaud-Sequeira A., Raldua D., Lavie J., Mathieu G., Bordier M.,
RA Knoll-Gellida A., Rambeau P., Coupry I., Andre M., Malm E., Moeller C.,
RA Andreasson S., Rendtorff N.D., Tranebjaerg L., Koenig M., Lacombe D.,
RA Goizet C., Babin P.J.;
RT "Functional validation of ABHD12 mutations in the neurodegenerative disease
RT PHARC.";
RL Neurobiol. Dis. 98:36-51(2017).
CC -!- FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the
CC hydrolysis of lysophosphatidylserine, a class of signaling lipids that
CC regulates immunological and neurological processes (By similarity).
CC Represents a major lysophosphatidylserine lipase in the brain, thereby
CC playing a key role in the central nervous system (By similarity). Also
CC able to hydrolyze oxidized phosphatidylserine; oxidized
CC phosphatidylserine is produced in response to severe inflammatory
CC stress and constitutes a proapoptotic 'eat me' signal. Also has
CC monoacylglycerol (MAG) lipase activity: hydrolyzes 2-
CC arachidonoylglycerol (2-AG), thereby acting as a regulator of
CC endocannabinoid signaling pathways. Has a strong preference for very-
CC long-chain lipid substrates; substrate specificity is likely due to
CC improved catalysis and not improved substrate binding (By similarity).
CC {ECO:0000250|UniProtKB:Q8N2K0, ECO:0000250|UniProtKB:Q99LR1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:44584, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64717,
CC ChEBI:CHEBI:72828; Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) +
CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-1D-myo-
CC inositol; Xref=Rhea:RHEA:44588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58444, ChEBI:CHEBI:78762;
CC Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) +
CC hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64765, ChEBI:CHEBI:75020;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75568;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75555; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9,10-epoxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine +
CC 9,10-epoxyoctadecanoate + H(+); Xref=Rhea:RHEA:59364,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467,
CC ChEBI:CHEBI:85195, ChEBI:CHEBI:143087;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine +
CC 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467,
CC ChEBI:CHEBI:143088, ChEBI:CHEBI:143089;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-L-serine
CC + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:143089, ChEBI:CHEBI:143094;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N2K0}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues.
CC {ECO:0000269|PubMed:27890673}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:27890673}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC myelination defects and functional deficits, characterized by
CC progressive ataxia and motor skill impairment (PubMed:27890673). A
CC disruption of retina architecture and retinotectal projections is
CC observed, together with an inhibition of lens clarification and a low
CC number of mechanosensory hair cells in the inner ear and lateral line
CC system (PubMed:27890673). {ECO:0000269|PubMed:27890673}.
CC -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR EMBL; BC124330; AAI24331.1; -; mRNA.
DR EMBL; AL953905; CAQ15102.1; -; Genomic_DNA.
DR RefSeq; NP_001070065.1; NM_001076597.1.
DR AlphaFoldDB; Q08C93; -.
DR SMR; Q08C93; -.
DR STRING; 7955.ENSDARP00000095479; -.
DR ESTHER; danre-q08c93; ABHD12-PHARC.
DR PaxDb; Q08C93; -.
DR PRIDE; Q08C93; -.
DR Ensembl; ENSDART00000104708; ENSDARP00000095479; ENSDARG00000071004.
DR GeneID; 767657; -.
DR KEGG; dre:767657; -.
DR CTD; 26090; -.
DR ZFIN; ZDB-GENE-060929-268; abhd12.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000166409; -.
DR HOGENOM; CLU_029375_1_0_1; -.
DR InParanoid; Q08C93; -.
DR OMA; YELHNCL; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q08C93; -.
DR TreeFam; TF315122; -.
DR Reactome; R-DRE-426048; Arachidonate production from DAG.
DR PRO; PR:Q08C93; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000071004; Expressed in swim bladder and 36 other tissues.
DR ExpressionAtlas; Q08C93; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0048899; P:anterior lateral line development; IMP:ZFIN.
DR GO; GO:0043010; P:camera-type eye development; IMP:ZFIN.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:ZFIN.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; ISS:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
DR GO; GO:0048919; P:posterior lateral line neuromast development; IMP:ZFIN.
DR GO; GO:0010842; P:retina layer formation; IMP:ZFIN.
DR GO; GO:0036269; P:swimming behavior; IMP:ZFIN.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR026605; ABHD12.
DR PANTHER; PTHR12277:SF61; PTHR12277:SF61; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..382
FT /note="Lysophosphatidylserine lipase ABHD12"
FT /id="PRO_0000375811"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT TOPO_DOM 82..382
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 319
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 382 AA; 43285 MW; E79E60CC2D743079 CRC64;
MRKRKGSADH DSSFTATLTD GSSDLKQCHK GTDADTDPGG SGKEMGRRCR RGGLMWRLRR
ILIWLLGIYI AIPVIIKVCP SIQAKLVFLN FVRVPYFIDL KRPQDQGMNH THNFYLQPEE
GINIGVWHTV PAGMWREAQA KDAEWYEKSF QSSHPVILYL HGNAGTRGGD HRVQLYKVLS
SLGYHVVTFD YRGWGDSEGS PSERGMTSDA LFLYQWIKQR IGPKPLYIWG HSLGTGVATN
LVRRLCDRGT PPDALILESP FTNIREEAKS HPFSMVYRYL PGFDWFFLDA ISANDIRFAS
DENVNHISCP VLILHAEDDT VVPFQLGKKL YDLAAQSKSL NGHKVQFIPF SSSLGYRHKF
IYKSPQLPNI LSDFLRAPHP HG
