PGAP3_HUMAN
ID PGAP3_HUMAN Reviewed; 320 AA.
AC Q96FM1; B4DGK7; Q86Z03; Q8NBJ8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Post-GPI attachment to proteins factor 3;
DE AltName: Full=COS16 homolog;
DE Short=hCOS16;
DE AltName: Full=Gene coamplified with ERBB2 protein;
DE AltName: Full=PER1-like domain-containing protein 1;
DE Flags: Precursor;
GN Name=PGAP3 {ECO:0000312|HGNC:HGNC:23719}; Synonyms=CAB2, PERLD1;
GN ORFNames=UNQ546/PRO1100;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12460457; DOI=10.1111/j.1349-7006.2002.tb01221.x;
RA Nezu M., Nishigaki M., Ishizuka T., Kuwahara Y., Tanabe C., Aoyagi K.,
RA Sakamoto H., Saito Y., Yoshida T., Sasaki H., Terada M.;
RT "Identification of the CAB2/hCOS16 gene required for the repair of DNA
RT double-strand breaks on a core amplified region of the 17q12 locus in
RT breast and gastric cancers.";
RL Jpn. J. Cancer Res. 93:1183-1186(2002).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [8]
RP IDENTIFICATION.
RX PubMed=12739007;
RA Katoh M., Katoh M.;
RT "MGC9753 gene, located within PPP1R1B-STARD3-ERBB2-GRB7 amplicon on human
RT chromosome 17q12, encodes the seven-transmembrane receptor with
RT extracellular six-cysteine domain.";
RL Int. J. Oncol. 22:1369-1374(2003).
RN [9]
RP FUNCTION.
RX PubMed=17021251; DOI=10.1091/mbc.e06-08-0715;
RA Fujita M., Umemura M., Yoko-o T., Jigami Y.;
RT "PER1 is required for GPI-phospholipase A2 activity and involved in lipid
RT remodeling of GPI-anchored proteins.";
RL Mol. Biol. Cell 17:5253-5264(2006).
RN [10]
RP FUNCTION.
RX PubMed=29374258; DOI=10.1038/s41467-017-02799-0;
RA Hirata T., Mishra S.K., Nakamura S., Saito K., Motooka D., Takada Y.,
RA Kanzawa N., Murakami Y., Maeda Y., Fujita M., Yamaguchi Y., Kinoshita T.;
RT "Identification of a Golgi GPI-N-acetylgalactosamine transferase with
RT tandem transmembrane regions in the catalytic domain.";
RL Nat. Commun. 9:405-405(2018).
RN [11]
RP VARIANTS HPMRS4 ASP-92; ARG-105 AND GLY-305, AND CHARACTERIZATION OF
RP VARIANTS HPMRS4 ASP-92; ARG-105 AND GLY-305.
RX PubMed=24439110; DOI=10.1016/j.ajhg.2013.12.012;
RA Howard M.F., Murakami Y., Pagnamenta A.T., Daumer-Haas C., Fischer B.,
RA Hecht J., Keays D.A., Knight S.J., Kolsch U., Kruger U., Leiz S., Maeda Y.,
RA Mitchell D., Mundlos S., Phillips J.A., Robinson P.N., Kini U.,
RA Taylor J.C., Horn D., Kinoshita T., Krawitz P.M.;
RT "Mutations in PGAP3 impair GPI-anchor maturation, causing a subtype of
RT hyperphosphatasia with mental retardation.";
RL Am. J. Hum. Genet. 94:278-287(2014).
RN [12]
RP VARIANT TYR-284.
RX PubMed=29620724; DOI=10.1038/gim.2018.50;
RA Maddirevula S., Alsahli S., Alhabeeb L., Patel N., Alzahrani F.,
RA Shamseldin H.E., Anazi S., Ewida N., Alsaif H.S., Mohamed J.Y.,
RA Alazami A.M., Ibrahim N., Abdulwahab F., Hashem M., Abouelhoda M.,
RA Monies D., Al Tassan N., Alshammari M., Alsagheir A., Seidahmed M.Z.,
RA Sogati S., Aglan M.S., Hamad M.H., Salih M.A., Hamed A.A., Alhashmi N.,
RA Nabil A., Alfadli F., Abdel-Salam G.M.H., Alkuraya H., Peitee W.O.,
RA Keng W.T., Qasem A., Mushiba A.M., Zaki M.S., Fassad M.R., Alfadhel M.,
RA Alexander S., Sabr Y., Temtamy S., Ekbote A.V., Ismail S., Hosny G.A.,
RA Otaify G.A., Amr K., Al Tala S., Khan A.O., Rizk T., Alaqeel A.,
RA Alsiddiky A., Singh A., Kapoor S., Alhashem A., Faqeih E., Shaheen R.,
RA Alkuraya F.S.;
RT "Expanding the phenome and variome of skeletal dysplasia.";
RL Genet. Med. 20:1609-1616(2018).
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. Lipid remodeling steps consist in the generation of 2
CC saturated fatty chains at the sn-2 position of GPI-anchors proteins.
CC Required for phospholipase A2 activity that removes an acyl-chain at
CC the sn-2 position of GPI-anchors during the remodeling of GPI.
CC {ECO:0000269|PubMed:29374258, ECO:0000305|PubMed:17021251}.
CC -!- INTERACTION:
CC Q96FM1; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-22113571, EBI-1054873;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:12460457}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:12460457}. Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:12460457}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:12460457}. Note=Mainly localizes to Golgi
CC apparatus. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96FM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FM1-2; Sequence=VSP_034158;
CC Name=3;
CC IsoId=Q96FM1-3; Sequence=VSP_057229;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC thyroid and placenta. {ECO:0000269|PubMed:12460457}.
CC -!- DISEASE: Hyperphosphatasia with intellectual disability syndrome 4
CC (HPMRS4) [MIM:615716]: An autosomal recessive neurologic disorder
CC characterized by profound developmental delay, severe intellectual
CC disability, no speech, psychomotor delay, postnatal microcephaly, and
CC elevated serum alkaline phosphatase. {ECO:0000269|PubMed:24439110}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: When transfected in S.cerevisiae, it can complement the
CC absence of yeast of PER1 protein, suggesting a conserved role in lipid
CC remodeling steps of GPI-anchor maturation.
CC -!- SIMILARITY: Belongs to the PGAP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC55580.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB088396; BAC55580.1; ALT_FRAME; mRNA.
DR EMBL; AY358437; AAQ88803.1; -; mRNA.
DR EMBL; AK294639; BAG57818.1; -; mRNA.
DR EMBL; AK075474; BAC11642.1; -; mRNA.
DR EMBL; AC087491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60592.1; -; Genomic_DNA.
DR EMBL; BC010652; AAH10652.2; -; mRNA.
DR CCDS; CCDS32641.1; -. [Q96FM1-1]
DR CCDS; CCDS77013.1; -. [Q96FM1-2]
DR CCDS; CCDS77015.1; -. [Q96FM1-3]
DR RefSeq; NP_001278655.1; NM_001291726.1. [Q96FM1-2]
DR RefSeq; NP_001278657.1; NM_001291728.1. [Q96FM1-3]
DR RefSeq; NP_001278659.1; NM_001291730.1.
DR RefSeq; NP_001278661.1; NM_001291732.1.
DR RefSeq; NP_001278662.1; NM_001291733.1.
DR RefSeq; NP_219487.3; NM_033419.4. [Q96FM1-1]
DR AlphaFoldDB; Q96FM1; -.
DR BioGRID; 125014; 9.
DR IntAct; Q96FM1; 3.
DR STRING; 9606.ENSP00000300658; -.
DR GlyConnect; 1621; 1 N-Linked glycan (1 site).
DR GlyGen; Q96FM1; 1 site, 1 N-linked glycan (1 site).
DR BioMuta; PGAP3; -.
DR DMDM; 74731724; -.
DR EPD; Q96FM1; -.
DR MassIVE; Q96FM1; -.
DR PaxDb; Q96FM1; -.
DR PeptideAtlas; Q96FM1; -.
DR PRIDE; Q96FM1; -.
DR ProteomicsDB; 4141; -.
DR ProteomicsDB; 76544; -. [Q96FM1-1]
DR ProteomicsDB; 76545; -. [Q96FM1-2]
DR Antibodypedia; 16261; 160 antibodies from 22 providers.
DR DNASU; 93210; -.
DR Ensembl; ENST00000300658.9; ENSP00000300658.4; ENSG00000161395.14. [Q96FM1-1]
DR Ensembl; ENST00000378011.8; ENSP00000367250.4; ENSG00000161395.14. [Q96FM1-2]
DR Ensembl; ENST00000429199.6; ENSP00000415765.2; ENSG00000161395.14. [Q96FM1-3]
DR GeneID; 93210; -.
DR KEGG; hsa:93210; -.
DR MANE-Select; ENST00000300658.9; ENSP00000300658.4; NM_033419.5; NP_219487.3.
DR UCSC; uc002hsj.4; human. [Q96FM1-1]
DR CTD; 93210; -.
DR DisGeNET; 93210; -.
DR GeneCards; PGAP3; -.
DR HGNC; HGNC:23719; PGAP3.
DR HPA; ENSG00000161395; Low tissue specificity.
DR MalaCards; PGAP3; -.
DR MIM; 611801; gene.
DR MIM; 615716; phenotype.
DR neXtProt; NX_Q96FM1; -.
DR OpenTargets; ENSG00000161395; -.
DR Orphanet; 247262; Hyperphosphatasia-intellectual disability syndrome.
DR PharmGKB; PA165432310; -.
DR VEuPathDB; HostDB:ENSG00000161395; -.
DR eggNOG; KOG2970; Eukaryota.
DR GeneTree; ENSGT00390000001304; -.
DR HOGENOM; CLU_032917_1_0_1; -.
DR InParanoid; Q96FM1; -.
DR OMA; FMIEDCR; -.
DR OrthoDB; 828384at2759; -.
DR PhylomeDB; Q96FM1; -.
DR TreeFam; TF300031; -.
DR PathwayCommons; Q96FM1; -.
DR SignaLink; Q96FM1; -.
DR BioGRID-ORCS; 93210; 16 hits in 1072 CRISPR screens.
DR ChiTaRS; PGAP3; human.
DR GenomeRNAi; 93210; -.
DR Pharos; Q96FM1; Tbio.
DR PRO; PR:Q96FM1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96FM1; protein.
DR Bgee; ENSG00000161395; Expressed in pancreatic ductal cell and 185 other tissues.
DR ExpressionAtlas; Q96FM1; baseline and differential.
DR Genevisible; Q96FM1; HS.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IMP:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006505; P:GPI anchor metabolic process; IMP:UniProtKB.
DR InterPro; IPR007217; Per1-like.
DR PANTHER; PTHR13148; PTHR13148; 1.
DR Pfam; PF04080; Per1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; GPI-anchor biosynthesis; Intellectual disability;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..320
FT /note="Post-GPI attachment to proteins factor 3"
FT /id="PRO_0000339356"
FT TOPO_DOM 21..98
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..169
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..224
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 94..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_034158"
FT VAR_SEQ 145..165
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057229"
FT VARIANT 92
FT /note="G -> D (in HPMRS4; results in loss of function; the
FT mutant localizes to the Golgi apparatus as the wild-type;
FT dbSNP:rs587777251)"
FT /evidence="ECO:0000269|PubMed:24439110"
FT /id="VAR_071155"
FT VARIANT 105
FT /note="P -> R (in HPMRS4; results in partial functional
FT impairment; the mutant does not localize to the Golgi
FT apparatus but is retained in the endoplasmic reticulum;
FT dbSNP:rs371549948)"
FT /evidence="ECO:0000269|PubMed:24439110"
FT /id="VAR_071156"
FT VARIANT 284
FT /note="H -> Y (found in a patient with Toriello-Carey
FT syndrome; unknown pathological significance;
FT dbSNP:rs759541820)"
FT /evidence="ECO:0000269|PubMed:29620724"
FT /id="VAR_084138"
FT VARIANT 305
FT /note="D -> G (in HPMRS4; results in partial functional
FT impairment; the mutant does not localize to the Golgi
FT apparatus but is retained in the endoplasmic reticulum;
FT dbSNP:rs587777252)"
FT /evidence="ECO:0000269|PubMed:24439110"
FT /id="VAR_071157"
FT CONFLICT 153
FT /note="S -> P (in Ref. 4; BAC11642)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="C -> R (in Ref. 4; BAC11642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 36475 MW; A5B0E170BF969C5A CRC64;
MAGLAARLVL LAGAAALASG SQGDREPVYR DCVLQCEEQN CSGGALNHFR SRQPIYMSLA
GWTCRDDCKY ECMWVTVGLY LQEGHKVPQF HGKWPFSRFL FFQEPASAVA SFLNGLASLV
MLCRYRTFVP ASSPMYHTCV AFAWVSLNAW FWSTVFHTRD TDLTEKMDYF CASTVILHSI
YLCCVRTVGL QHPAVVSAFR ALLLLMLTVH VSYLSLIRFD YGYNLVANVA IGLVNVVWWL
AWCLWNQRRL PHVRKCVVVV LLLQGLSLLE LLDFPPLFWV LDAHAIWHIS TIPVHVLFFS
FLEDDSLYLL KESEDKFKLD
