GPHRA_HUMAN
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 03-AUG-2022, entry version 96.
DE RecName: Full=Golgi pH regulator A;
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; 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), AND FUNCTION.
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, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE 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 dependent anion channel required for acidification
CC and functions of the Golgi apparatus that may function in counter-ion
CC conductance (PubMed:12761501, PubMed:18794847). Plays a role in
CC lymphocyte development, probably by acting as a RABL3 effector in
CC hematopoietic cells (By similarity). {ECO:0000250|UniProtKB:Q8BS95,
CC ECO:0000269|PubMed:12761501, 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:0000250|UniProtKB:B2ZXD5}; 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 -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family.
CC {ECO:0000305}.
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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. [B7ZAQ6-2]
DR RefSeq; XP_011507912.1; XM_011509610.2.
DR RefSeq; XP_011507914.1; XM_011509612.2. [B7ZAQ6-2]
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. [B7ZAQ6-3]
DR AlphaFoldDB; B7ZAQ6; -.
DR SMR; B7ZAQ6; -.
DR BioGRID; 119554; 33.
DR BioGRID; 575849; 126.
DR IntAct; B7ZAQ6; 40.
DR STRING; 9606.ENSP00000319673; -.
DR GlyGen; B7ZAQ6; 2 sites.
DR iPTMnet; B7ZAQ6; -.
DR PhosphoSitePlus; B7ZAQ6; -.
DR SwissPalm; B7ZAQ6; -.
DR BioMuta; GPR89A; -.
DR EPD; B7ZAQ6; -.
DR jPOST; B7ZAQ6; -.
DR MassIVE; B7ZAQ6; -.
DR MaxQB; B7ZAQ6; -.
DR PaxDb; B7ZAQ6; -.
DR PRIDE; B7ZAQ6; -.
DR ProteomicsDB; 7078; -. [B7ZAQ6-2]
DR ProteomicsDB; 7079; -. [B7ZAQ6-3]
DR Antibodypedia; 10137; 138 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 MANE-Select; ENST00000314163.12; ENSP00000358233.4; NM_016334.5; NP_057418.1.
DR UCSC; uc010ozb.2; human. [B7ZAQ6-1]
DR CTD; 51463; -.
DR CTD; 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; HFNFYHR; -.
DR OrthoDB; 1065554at2759; -.
DR PhylomeDB; B7ZAQ6; -.
DR TreeFam; TF313484; -.
DR PathwayCommons; B7ZAQ6; -.
DR SignaLink; B7ZAQ6; -.
DR BioGRID-ORCS; 51463; 94 hits in 629 CRISPR screens.
DR BioGRID-ORCS; 653519; 244 hits in 988 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 103 other tissues.
DR ExpressionAtlas; B7ZAQ6; baseline and differential.
DR Genevisible; B7ZAQ6; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR GO; GO:0051452; P:intracellular pH reduction; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034765; P:regulation of ion transmembrane 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; PTHR15948; 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
