GPR37_HUMAN
ID GPR37_HUMAN Reviewed; 613 AA.
AC O15354; A4D0Y6; O00348; O14768; Q8TD39;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Prosaposin receptor GPR37;
DE AltName: Full=Endothelin B receptor-like protein 1;
DE Short=ETBR-LP-1;
DE AltName: Full=G-protein coupled receptor 37;
DE AltName: Full=Parkin-associated endothelin receptor-like receptor;
DE Short=PAELR;
DE Flags: Precursor;
GN Name=GPR37;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9339362; DOI=10.1006/geno.1997.4900;
RA Marazziti D., Golini E., Gallo A., Lombardi M.S., Matteoni R.,
RA Tocchini-Valentini G.P.;
RT "Cloning of GPR37, a gene located on chromosome 7 encoding a putative G-
RT protein-coupled peptide receptor, from a human frontal brain EST library.";
RL Genomics 45:68-77(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9526070; DOI=10.1016/s0169-328x(97)00336-7;
RA Donohue P.J., Shapira H., Mantey S.A., Hampton L.L., Jensen R.T.,
RA Battey J.F.;
RT "A human gene encodes a putative G protein-coupled receptor highly
RT expressed in the central nervous system.";
RL Brain Res. Mol. Brain Res. 54:152-160(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9144577; DOI=10.1006/bbrc.1997.6408;
RA Zeng Z., Su K., Kyaw H., Li Y.;
RT "A novel endothelin receptor type-B-like gene enriched in the brain.";
RL Biochem. Biophys. Res. Commun. 233:559-567(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PRKN.
RC TISSUE=Brain;
RX PubMed=11439185; DOI=10.1016/s0092-8674(01)00407-x;
RA Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R.;
RT "An unfolded putative transmembrane polypeptide, which can lead to
RT endoplasmic reticulum stress, is a substrate of Parkin.";
RL Cell 105:891-902(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH PRKN; STUB1 AND HSP70.
RX PubMed=12150907; DOI=10.1016/s1097-2765(02)00583-x;
RA Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.,
RA Takahashi R.;
RT "CHIP is associated with Parkin, a gene responsible for familial
RT Parkinson's disease, and enhances its ubiquitin ligase activity.";
RL Mol. Cell 10:55-67(2002).
RN [10]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.m309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [11]
RP UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=17059562; DOI=10.1111/j.1471-4159.2006.04155.x;
RA Omura T., Kaneko M., Okuma Y., Orba Y., Nagashima K., Takahashi R.,
RA Fujitani N., Matsumura S., Hata A., Kubota K., Murahashi K., Uehara T.,
RA Nomura Y.;
RT "A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a
RT substrate of Parkin.";
RL J. Neurochem. 99:1456-1469(2006).
RN [12]
RP FUNCTION.
RX PubMed=23690594; DOI=10.1073/pnas.1219004110;
RA Meyer R.C., Giddens M.M., Schaefer S.A., Hall R.A.;
RT "GPR37 and GPR37L1 are receptors for the neuroprotective and glioprotective
RT factors prosaptide and prosaposin.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9529-9534(2013).
CC -!- FUNCTION: Receptor for the neuroprotective and glioprotective factor
CC prosaposin. Ligand binding induces endocytosis, followed by an ERK
CC phosphorylation cascade. {ECO:0000269|PubMed:11439185,
CC ECO:0000269|PubMed:23690594, ECO:0000269|PubMed:9526070}.
CC -!- SUBUNIT: Forms a complex with PRKN, STUB1 and HSP70. The amount of
CC STUB1 in the complex increases during ER stress. STUB1 promotes the
CC dissociation of HSP70 from PRKN, thus facilitating PRKN-mediated GPR37
CC ubiquitination. Interacts with PACRG. {ECO:0000269|PubMed:11439185,
CC ECO:0000269|PubMed:12150907, ECO:0000269|PubMed:14532270}.
CC -!- INTERACTION:
CC O15354; P29274: ADORA2A; NbExp=3; IntAct=EBI-15639515, EBI-2902702;
CC O15354; D3DTF8: APLN; NbExp=3; IntAct=EBI-15639515, EBI-22002556;
CC O15354; Q02930-3: CREB5; NbExp=3; IntAct=EBI-15639515, EBI-10192698;
CC O15354; O15540: FABP7; NbExp=3; IntAct=EBI-15639515, EBI-10697159;
CC O15354; Q5HYJ3-3: FAM76B; NbExp=3; IntAct=EBI-15639515, EBI-11956087;
CC O15354; Q9UBS5: GABBR1; NbExp=2; IntAct=EBI-15639515, EBI-724156;
CC O15354; Q13639: HTR4; NbExp=5; IntAct=EBI-15639515, EBI-6656425;
CC O15354; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-15639515, EBI-10246607;
CC O15354; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-15639515, EBI-10699187;
CC O15354; Q14995: NR1D2; NbExp=3; IntAct=EBI-15639515, EBI-6144053;
CC O15354; Q14671: PUM1; NbExp=3; IntAct=EBI-15639515, EBI-948453;
CC O15354; Q7Z7K5: PXN; NbExp=3; IntAct=EBI-15639515, EBI-25841978;
CC O15354; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-15639515, EBI-4403649;
CC O15354; P34741: SDC2; NbExp=3; IntAct=EBI-15639515, EBI-1172957;
CC O15354; P08195: SLC3A2; NbExp=3; IntAct=EBI-15639515, EBI-702356;
CC O15354; Q01959: SLC6A3; NbExp=2; IntAct=EBI-15639515, EBI-6661445;
CC O15354; A0A024R4B0: SPATA3; NbExp=3; IntAct=EBI-15639515, EBI-14123856;
CC O15354; Q9NX61: TMEM161A; NbExp=2; IntAct=EBI-15639515, EBI-6138599;
CC O15354; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-15639515, EBI-25831574;
CC O15354; Q9H313: TTYH1; NbExp=2; IntAct=EBI-15639515, EBI-20793786;
CC O15354; O95070: YIF1A; NbExp=2; IntAct=EBI-15639515, EBI-2799703;
CC O15354; Q5BJH7: YIF1B; NbExp=2; IntAct=EBI-15639515, EBI-11288011;
CC O15354; P25490: YY1; NbExp=3; IntAct=EBI-15639515, EBI-765538;
CC O15354; Q9C0A1: ZFHX2; NbExp=3; IntAct=EBI-15639515, EBI-25850811;
CC O15354; Q7L8T7; NbExp=3; IntAct=EBI-15639515, EBI-25831943;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17059562};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17059562}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:17059562}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and spinal cord, and at lower
CC levels in testis, placenta and liver, but no detectable expression
CC observed in any other tissue. When overexpressed in cells, tends to
CC become insoluble and unfolded. Accumulation of the unfolded protein may
CC lead to dopaminergic neuronal death in juvenile Parkinson disease
CC (PDJ). {ECO:0000269|PubMed:9526070}.
CC -!- PTM: Ubiquitinated by PRKN in the presence of UBE2E1 and UBE2L3 in the
CC endoplasmic reticulum. The unfolded form is specifically ubiquitinated
CC by SYVN1, which promotes its proteasomal degradation and prevents
CC neuronal cell death. {ECO:0000269|PubMed:17059562}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Y12476; CAA73080.1; -; Genomic_DNA.
DR EMBL; Y12477; CAA73080.1; JOINED; Genomic_DNA.
DR EMBL; AF017262; AAB70008.1; -; mRNA.
DR EMBL; U87460; AAC51281.1; -; mRNA.
DR EMBL; AF502281; AAM18625.2; -; mRNA.
DR EMBL; AC004925; AAD08853.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24325.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83613.1; -; Genomic_DNA.
DR EMBL; BC040007; AAH40007.1; -; mRNA.
DR CCDS; CCDS5792.1; -.
DR PIR; JC5501; JC5501.
DR RefSeq; NP_005293.1; NM_005302.3.
DR AlphaFoldDB; O15354; -.
DR SMR; O15354; -.
DR BioGRID; 109119; 93.
DR DIP; DIP-60954N; -.
DR IntAct; O15354; 71.
DR MINT; O15354; -.
DR STRING; 9606.ENSP00000306449; -.
DR ChEMBL; CHEMBL4523862; -.
DR GuidetoPHARMACOLOGY; 103; -.
DR TCDB; 9.A.14.13.20; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; O15354; 3 sites.
DR iPTMnet; O15354; -.
DR PhosphoSitePlus; O15354; -.
DR BioMuta; GPR37; -.
DR EPD; O15354; -.
DR jPOST; O15354; -.
DR MassIVE; O15354; -.
DR PaxDb; O15354; -.
DR PeptideAtlas; O15354; -.
DR PRIDE; O15354; -.
DR ProteomicsDB; 48607; -.
DR Antibodypedia; 17671; 312 antibodies from 35 providers.
DR DNASU; 2861; -.
DR Ensembl; ENST00000303921.3; ENSP00000306449.2; ENSG00000170775.3.
DR GeneID; 2861; -.
DR KEGG; hsa:2861; -.
DR MANE-Select; ENST00000303921.3; ENSP00000306449.2; NM_005302.5; NP_005293.1.
DR UCSC; uc003vli.5; human.
DR CTD; 2861; -.
DR DisGeNET; 2861; -.
DR GeneCards; GPR37; -.
DR HGNC; HGNC:4494; GPR37.
DR HPA; ENSG00000170775; Group enriched (brain, retina).
DR MIM; 602583; gene.
DR neXtProt; NX_O15354; -.
DR OpenTargets; ENSG00000170775; -.
DR PharmGKB; PA28882; -.
DR VEuPathDB; HostDB:ENSG00000170775; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01040000240430; -.
DR HOGENOM; CLU_032138_1_0_1; -.
DR InParanoid; O15354; -.
DR OMA; CLGENCS; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; O15354; -.
DR TreeFam; TF331292; -.
DR PathwayCommons; O15354; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O15354; -.
DR SIGNOR; O15354; -.
DR BioGRID-ORCS; 2861; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; GPR37; human.
DR GeneWiki; GPR37; -.
DR GenomeRNAi; 2861; -.
DR Pharos; O15354; Tbio.
DR PRO; PR:O15354; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15354; protein.
DR Bgee; ENSG00000170775; Expressed in secondary oocyte and 131 other tissues.
DR Genevisible; O15354; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0031072; F:heat shock protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042923; F:neuropeptide binding; IPI:UniProtKB.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0042277; F:peptide binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0036505; F:prosaposin receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IEA:Ensembl.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ParkinsonsUK-UCL.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003909; GPR37_orph.
DR PANTHER; PTHR46216; PTHR46216; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01421; GPR37ORPHANR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..613
FT /note="Prosaposin receptor GPR37"
FT /id="PRO_0000012799"
FT TOPO_DOM 27..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 80..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 93
FT /note="G -> D (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="A -> T (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="G -> V (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> V (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="W -> C (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="E -> D (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="C -> S (in Ref. 2; AAB70008)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="A -> V (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="L -> V (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..504
FT /note="FC -> LG (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="T -> A (in Ref. 3; AAC51281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67114 MW; 5A1AB269ED63E765 CRC64;
MRAPGALLAR MSRLLLLLLL KVSASSALGV APASRNETCL GESCAPTVIQ RRGRDAWGPG
NSARDVLRAR APREEQGAAF LAGPSWDLPA APGRDPAAGR GAEASAAGPP GPPTRPPGPW
RWKGARGQEP SETLGRGNPT ALQLFLQISE EEEKGPRGAG ISGRSQEQSV KTVPGASDLF
YWPRRAGKLQ GSHHKPLSKT ANGLAGHEGW TIALPGRALA QNGSLGEGIH EPGGPRRGNS
TNRRVRLKNP FYPLTQESYG AYAVMCLSVV IFGTGIIGNL AVMCIVCHNY YMRSISNSLL
ANLAFWDFLI IFFCLPLVIF HELTKKWLLE DFSCKIVPYI EVASLGVTTF TLCALCIDRF
RAATNVQMYY EMIENCSSTT AKLAVIWVGA LLLALPEVVL RQLSKEDLGF SGRAPAERCI
IKISPDLPDT IYVLALTYDS ARLWWYFGCY FCLPTLFTIT CSLVTARKIR KAEKACTRGN
KRQIQLESQM NCTVVALTIL YGFCIIPENI CNIVTAYMAT GVSQQTMDLL NIISQFLLFF
KSCVTPVLLF CLCKPFSRAF MECCCCCCEE CIQKSSTVTS DDNDNEYTTE LELSPFSTIR
REMSTFASVG THC
