ID GPHRA_HUMAN Reviewed; 455 AA. AC B7ZAQ6; A6NN37; B2RUV3; B3KMN3; B4DLT3; B4DXE7; Q53FQ9; Q5T2V8; Q5T5P5; AC Q659E2; Q6NVY5; Q9P0S4; Q9Y302; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 2. DT 02-OCT-2024, entry version 108. DE RecName: Full=Golgi pH regulator A {ECO:0000305}; DE AltName: Full=Protein GPR89A; DE AltName: Full=Putative MAPK-activating protein PM01; DE AltName: Full=Putative NF-kappa-B-activating protein 90; GN Name=GPR89A {ECO:0000312|HGNC:HGNC:31984}; GN Synonyms=GPHRA, GPR89, SH120; ORFNames=CGI-13, UNQ192/PRO218; 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 [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=24722188; DOI=10.1038/ncomms4650; RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.; RT "Protein interaction network of alternatively spliced isoforms from brain RT links genetic risk factors for autism."; RL Nat. Commun. 5:3650-3650(2014). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung fibroblast; RX PubMed=12761501; DOI=10.1038/sj.onc.1206406; RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.; RT "Large-scale identification and characterization of human genes that RT activate NF-kappaB and MAPK signaling pathways."; RL Oncogene 22:3307-3318(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Embryo, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Lung, and Testis; 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 [10] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE RP SPECIFICITY. RX PubMed=18794847; DOI=10.1038/ncb1773; RA Maeda Y., Ide T., Koike M., Uchiyama Y., Kinoshita T.; RT "GPHR is a novel anion channel critical for acidification and functions of RT the Golgi apparatus."; RL Nat. Cell Biol. 10:1135-1145(2008). RN [11] RP LACK OF GTP-BINDING. RX PubMed=19135895; DOI=10.1016/j.cell.2008.12.026; RA Pandey S., Nelson D.C., Assmann S.M.; RT "Two novel GPCR-type G proteins are abscisic acid receptors in RT Arabidopsis."; RL Cell 136:136-148(2009). CC -!- FUNCTION: Voltage-gated channel that enables the transfer of monoatomic CC anions such as iodide, chloride, bromide and fluoride which may CC function in counter-ion conductance and participates in Golgi CC acidification (PubMed:18794847). Plays a role in lymphocyte CC development, probably by acting as a RABL3 effector in hematopoietic CC cells (By similarity). {ECO:0000250|UniProtKB:Q8BS95, CC ECO:0000269|PubMed:18794847}. CC -!- CATALYTIC ACTIVITY: CC Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, CC ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:18794847}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:18794847}; CC -!- CATALYTIC ACTIVITY: CC Reaction=bromide(in) = bromide(out); Xref=Rhea:RHEA:75383, CC ChEBI:CHEBI:15858; Evidence={ECO:0000269|PubMed:18794847}; CC -!- CATALYTIC ACTIVITY: CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, CC ChEBI:CHEBI:17051; Evidence={ECO:0000269|PubMed:18794847}; CC -!- SUBUNIT: Homotrimer (PubMed:18794847). Interacts with RABL3; the CC interaction stabilizes GPR89A (By similarity). CC {ECO:0000250|UniProtKB:Q8BS95, ECO:0000269|PubMed:18794847}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:18794847}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=B7ZAQ6-1; Sequence=Displayed; CC Name=2; CC IsoId=B7ZAQ6-2; Sequence=VSP_017247; CC Name=3; CC IsoId=B7ZAQ6-3; Sequence=VSP_039346; CC Name=4; Synonyms=A; CC IsoId=B7ZAQ6-4; Sequence=VSP_055892, VSP_055893; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18794847}. CC -!- MISCELLANEOUS: Does not seem to be able to bind GTP. CC {ECO:0000269|PubMed:19135895}. CC -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF132947; AAD27722.1; -; mRNA. DR EMBL; KJ535049; AHW56688.1; -; mRNA. DR EMBL; AY358966; AAQ89325.1; -; mRNA. DR EMBL; AB097024; BAC77377.1; -; mRNA. DR EMBL; AB097025; BAC77378.1; -; mRNA. DR EMBL; BT006679; AAP35325.1; -; mRNA. DR EMBL; AK021758; BAG51045.1; -; mRNA. DR EMBL; AK297145; BAG59645.1; -; mRNA. DR EMBL; AK301939; BAG63359.1; -; mRNA. DR EMBL; AK316371; BAH14742.1; -; mRNA. DR EMBL; AK223223; BAD96943.1; -; mRNA. DR EMBL; AL390725; CAI13712.2; -; Genomic_DNA. DR EMBL; BX511042; CAI13712.2; JOINED; Genomic_DNA. DR EMBL; CR628408; CAI13712.2; JOINED; Genomic_DNA. DR EMBL; BX511042; CAI13224.2; -; Genomic_DNA. DR EMBL; AL390725; CAI13224.2; JOINED; Genomic_DNA. DR EMBL; CR628408; CAI13224.2; JOINED; Genomic_DNA. DR EMBL; CR628408; CAM28366.1; -; Genomic_DNA. DR EMBL; AL390725; CAM28366.1; JOINED; Genomic_DNA. DR EMBL; BX511042; CAM28366.1; JOINED; Genomic_DNA. DR EMBL; BC003187; AAH03187.1; -; mRNA. DR EMBL; BC067816; AAH67816.1; -; mRNA. DR EMBL; BC146880; AAI46881.1; -; mRNA. DR CCDS; CCDS72857.1; -. [B7ZAQ6-1] DR CCDS; CCDS72858.1; -. [B7ZAQ6-3] DR RefSeq; NP_001091081.1; NM_001097612.1. [B7ZAQ6-1] DR RefSeq; NP_001091082.2; NM_001097613.2. [B7ZAQ6-3] DR RefSeq; NP_057418.1; NM_016334.3. [B7ZAQ6-1] DR RefSeq; XP_005277458.1; XM_005277401.3. DR RefSeq; XP_005277459.1; XM_005277402.4. [B7ZAQ6-3] DR RefSeq; XP_005277461.1; XM_005277404.3. DR RefSeq; XP_006711440.1; XM_006711377.3. DR RefSeq; XP_006711441.1; XM_006711378.2. DR RefSeq; XP_006711555.1; XM_006711492.3. [B7ZAQ6-1] DR RefSeq; XP_006711556.1; XM_006711493.3. DR RefSeq; XP_011507912.1; XM_011509610.2. DR RefSeq; XP_011507914.1; XM_011509612.2. DR RefSeq; XP_011508210.1; XM_011509908.2. [B7ZAQ6-3] DR RefSeq; XP_011508211.1; XM_011509909.2. [B7ZAQ6-3] DR RefSeq; XP_016856937.1; XM_017001448.1. DR AlphaFoldDB; B7ZAQ6; -. DR SMR; B7ZAQ6; -. DR BioGRID; 119554; 50. DR BioGRID; 575849; 132. DR IntAct; B7ZAQ6; 92. DR STRING; 9606.ENSP00000319673; -. DR GlyCosmos; B7ZAQ6; 2 sites, No reported glycans. DR GlyGen; B7ZAQ6; 2 sites. DR iPTMnet; B7ZAQ6; -. DR PhosphoSitePlus; B7ZAQ6; -. DR SwissPalm; B7ZAQ6; -. DR BioMuta; GPR89A; -. DR jPOST; B7ZAQ6; -. DR MassIVE; B7ZAQ6; -. DR PaxDb; 9606-ENSP00000319673; -. DR ProteomicsDB; 7078; -. [B7ZAQ6-2] DR ProteomicsDB; 7079; -. [B7ZAQ6-3] DR Pumba; B7ZAQ6; -. DR Antibodypedia; 10137; 152 antibodies from 18 providers. DR DNASU; 51463; -. DR Ensembl; ENST00000313835.14; ENSP00000319673.9; ENSG00000117262.19. [B7ZAQ6-1] DR Ensembl; ENST00000460277.5; ENSP00000436705.1; ENSG00000117262.19. [B7ZAQ6-4] DR Ensembl; ENST00000462900.2; ENSP00000432248.1; ENSG00000117262.19. [B7ZAQ6-3] DR Ensembl; ENST00000528944.5; ENSP00000434108.1; ENSG00000117262.19. [B7ZAQ6-4] DR Ensembl; ENST00000534502.5; ENSP00000434495.1; ENSG00000117262.19. [B7ZAQ6-3] DR GeneID; 51463; -. DR GeneID; 653519; -. DR KEGG; hsa:51463; -. DR KEGG; hsa:653519; -. DR MANE-Select; ENST00000313835.14; ENSP00000319673.9; NM_001097612.2; NP_001091081.1. DR UCSC; uc010ozb.2; human. [B7ZAQ6-1] DR AGR; HGNC:13840; -. DR AGR; HGNC:31984; -. DR CTD; 51463; -. DR CTD; 653519; -. DR DisGeNET; 653519; -. DR GeneCards; GPR89A; -. DR HGNC; HGNC:31984; GPR89A. DR HPA; ENSG00000117262; Low tissue specificity. DR MIM; 612821; gene. DR neXtProt; NX_B7ZAQ6; -. DR PharmGKB; PA134986137; -. DR VEuPathDB; HostDB:ENSG00000117262; -. DR eggNOG; KOG2417; Eukaryota. DR GeneTree; ENSGT00390000000684; -. DR HOGENOM; CLU_2003122_0_0_1; -. DR InParanoid; B7ZAQ6; -. DR OMA; FSVYCVY; -. DR OrthoDB; 90523at2759; -. DR PhylomeDB; B7ZAQ6; -. DR TreeFam; TF313484; -. DR PathwayCommons; B7ZAQ6; -. DR SignaLink; B7ZAQ6; -. DR BioGRID-ORCS; 51463; 102 hits in 680 CRISPR screens. DR BioGRID-ORCS; 653519; 250 hits in 1041 CRISPR screens. DR ChiTaRS; GPR89A; human. DR GeneWiki; GPR89B; -. DR Pharos; B7ZAQ6; Tbio. DR PRO; PR:B7ZAQ6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; B7ZAQ6; protein. DR Bgee; ENSG00000117262; Expressed in corpus callosum and 104 other cell types or tissues. DR ExpressionAtlas; B7ZAQ6; baseline and differential. DR GO; GO:0032580; C:Golgi cisterna membrane; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB. DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW. DR GO; GO:0008308; F:voltage-gated monoatomic anion channel activity; IDA:UniProtKB. DR GO; GO:0051452; P:intracellular pH reduction; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB. DR InterPro; IPR025969; ABA_GPCR_dom. DR InterPro; IPR022535; Golgi_pH-regulator_cons_dom. DR InterPro; IPR015672; GPHR/GTG. DR PANTHER; PTHR15948; G-PROTEIN COUPLED RECEPTOR 89-RELATED; 1. DR PANTHER; PTHR15948:SF0; GOLGI PH REGULATOR A-RELATED; 1. DR Pfam; PF12430; ABA_GPCR; 1. DR Pfam; PF12537; GPHR_N; 1. PE 1: Evidence at protein level; KW Alternative splicing; Glycoprotein; Golgi apparatus; Ion channel; KW Ion transport; Membrane; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..455 FT /note="Golgi pH regulator A" FT /id="PRO_0000223260" FT TRANSMEM 5..25 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 46..66 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 343..363 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 378..398 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 425..445 FT /note="Helical" FT /evidence="ECO:0000255" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 243 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..120 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_017247" FT VAR_SEQ 1..25 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039346" FT VAR_SEQ 106..124 FT /note="HKQRLLFSCLLWLTFMYFF -> LSPLSQCINNDCFFPVSYG (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:24722188" FT /id="VSP_055892" FT VAR_SEQ 125..455 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:24722188" FT /id="VSP_055893" FT CONFLICT 100 FT /note="S -> G (in Ref. 6; BAG63359)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="N -> MPD (in Ref. 7; BAD96943)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="I -> T (in Ref. 7; BAD96943)" FT /evidence="ECO:0000305" SQ SEQUENCE 455 AA; 52917 MW; D831F66E682643F9 CRC64; MSFLIDSSIM ITSQILFFGF GWLFFMRQLF KDYEIRQYVV QVIFSVTFAF SCTMFELIIF EILGVLNSSS RYFHWKMNLC VILLILVFMV PFYIGYFIVS NIRLLHKQRL LFSCLLWLTF MYFFWKLGDP FPILSPKHGI LSIEQLISRV GVIGVTLMAL LSGFGAVNCP YTYMSYFLRN VTDTDILALE RRLLQTMDMI ISKKKRMAMA RRTMFQKGEV HNKPSGFWGM IKSVTTSASG SENLTLIQQE VDALEELSRQ LFLETADLYA TKERIEYSKT FKGKYFNFLG YFFSIYCVWK IFMATINIVF DRVGKTDPVT RGIEITVNYL GIQFDVKFWS QHISFILVGI IIVTSIRGLL ITLTKFFYAI SSSKSSNVIV LLLAQIMGMY FVSSVLLIRM SMPLEYRTII TEVLGELQFN FYHRWFDVIF LVSALSSILF LYLAHKQAPE KQMAP //