PGAP2_HUMAN
ID PGAP2_HUMAN Reviewed; 254 AA.
AC Q9UHJ9; E9PJG5; H7BXL9; Q6UC77; Q96G66; Q9UF01; Q9Y4N1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Post-GPI attachment to proteins factor 2 {ECO:0000305};
DE AltName: Full=FGF receptor-activating protein 1;
GN Name=PGAP2 {ECO:0000312|HGNC:HGNC:17893}; Synonyms=FRAG1;
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 / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=10585768; DOI=10.1006/geno.1999.5980;
RA Lorenzi M.V., Castagnino P., Aaronson D.C., Lieb D.C., Lee C.C., Keck C.L.,
RA Popescu N.C., Miki T.;
RT "Human FRAG1 encodes a novel membrane-spanning protein that localizes to
RT chromosome 11p15.5, a region of frequent loss of heterozygosity in
RT cancer.";
RL Genomics 62:59-66(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Zhou G., Yu R., Zhong G., Li H., Shen C., Zheng G., Ke R., Lin L., Yang S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(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 3).
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-55.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
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 [10]
RP VARIANTS HPMRS3 CYS-99 AND PRO-177, AND TOPOLOGY.
RX PubMed=23561846; DOI=10.1016/j.ajhg.2013.03.008;
RA Hansen L., Tawamie H., Murakami Y., Mang Y., ur Rehman S., Buchert R.,
RA Schaffer S., Muhammad S., Bak M., Nothen M.M., Bennett E.P., Maeda Y.,
RA Aigner M., Reis A., Kinoshita T., Tommerup N., Baig S.M., Abou Jamra R.;
RT "Hypomorphic mutations in PGAP2, encoding a GPI-anchor-remodeling protein,
RT cause autosomal-recessive intellectual disability.";
RL Am. J. Hum. Genet. 92:575-583(2013).
RN [11]
RP VARIANTS HPMRS3 TRP-16; SER-127 AND ILE-160.
RX PubMed=23561847; DOI=10.1016/j.ajhg.2013.03.011;
RA Krawitz P.M., Murakami Y., Riess A., Hietala M., Kruger U., Zhu N.,
RA Kinoshita T., Mundlos S., Hecht J., Robinson P.N., Horn D.;
RT "PGAP2 mutations, affecting the GPI-anchor-synthesis pathway, cause
RT hyperphosphatasia with mental retardation syndrome.";
RL Am. J. Hum. Genet. 92:584-589(2013).
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. Required for stable expression of GPI-anchored proteins at
CC the cell surface. {ECO:0000269|PubMed:29374258}.
CC -!- SUBUNIT: Interacts with PGAP2IP. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UHJ9; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10321427, EBI-6942903;
CC Q9UHJ9; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10321427, EBI-10172052;
CC Q9UHJ9-5; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-12092917, EBI-19125216;
CC Q9UHJ9-5; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12092917, EBI-11343438;
CC Q9UHJ9-5; Q13323: BIK; NbExp=3; IntAct=EBI-12092917, EBI-700794;
CC Q9UHJ9-5; P11912: CD79A; NbExp=3; IntAct=EBI-12092917, EBI-7797864;
CC Q9UHJ9-5; Q99675: CGRRF1; NbExp=3; IntAct=EBI-12092917, EBI-2130213;
CC Q9UHJ9-5; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12092917, EBI-1045797;
CC Q9UHJ9-5; O95471: CLDN7; NbExp=3; IntAct=EBI-12092917, EBI-740744;
CC Q9UHJ9-5; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-12092917, EBI-11291074;
CC Q9UHJ9-5; P21964: COMT; NbExp=3; IntAct=EBI-12092917, EBI-372265;
CC Q9UHJ9-5; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12092917, EBI-18013275;
CC Q9UHJ9-5; Q96BA8: CREB3L1; NbExp=6; IntAct=EBI-12092917, EBI-6942903;
CC Q9UHJ9-5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12092917, EBI-3867333;
CC Q9UHJ9-5; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12092917, EBI-781551;
CC Q9UHJ9-5; Q9Y624: F11R; NbExp=3; IntAct=EBI-12092917, EBI-742600;
CC Q9UHJ9-5; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12092917, EBI-18304435;
CC Q9UHJ9-5; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12092917, EBI-12142257;
CC Q9UHJ9-5; P36382: GJA5; NbExp=3; IntAct=EBI-12092917, EBI-750433;
CC Q9UHJ9-5; P48165: GJA8; NbExp=3; IntAct=EBI-12092917, EBI-17458373;
CC Q9UHJ9-5; O95377: GJB5; NbExp=3; IntAct=EBI-12092917, EBI-3909454;
CC Q9UHJ9-5; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12092917, EBI-13345167;
CC Q9UHJ9-5; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12092917, EBI-11721746;
CC Q9UHJ9-5; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-12092917, EBI-749265;
CC Q9UHJ9-5; Q9HCJ2: LRRC4C; NbExp=3; IntAct=EBI-12092917, EBI-3925442;
CC Q9UHJ9-5; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12092917, EBI-716063;
CC Q9UHJ9-5; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12092917, EBI-17280858;
CC Q9UHJ9-5; Q16623: STX1A; NbExp=3; IntAct=EBI-12092917, EBI-712466;
CC Q9UHJ9-5; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12092917, EBI-18178701;
CC Q9UHJ9-5; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-12092917, EBI-723976;
CC Q9UHJ9-5; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-12092917, EBI-12345267;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2;
CC IsoId=Q9UHJ9-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UHJ9-2; Sequence=VSP_032550;
CC Name=3;
CC IsoId=Q9UHJ9-3; Sequence=VSP_032551;
CC Name=4;
CC IsoId=Q9UHJ9-4; Sequence=VSP_045984, VSP_045985;
CC Name=5;
CC IsoId=Q9UHJ9-5; Sequence=VSP_053800, VSP_032551;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis and pancreas. {ECO:0000269|PubMed:10585768}.
CC -!- DISEASE: Hyperphosphatasia with intellectual disability syndrome 3
CC (HPMRS3) [MIM:614207]: An autosomal recessive disorder usually
CC characterized by intellectual disability, hypotonia with very poor
CC motor development, poor speech, and increased serum alkaline
CC phosphatase. {ECO:0000269|PubMed:23561846,
CC ECO:0000269|PubMed:23561847}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: This isoform is predicted to contain an
CC additional transmembrane domain at position 85-105. If this domain
CC exists, the topology of the protein would be modified, possibly
CC challenging the GPI-anchor remodeling function of the protein.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PGAP2 family. {ECO:0000305}.
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DR EMBL; AF159615; AAF12755.1; -; mRNA.
DR EMBL; BX379511; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY373030; AAQ75733.1; -; mRNA.
DR EMBL; AF159621; AAF19156.1; -; Genomic_DNA.
DR EMBL; AF159616; AAF19156.1; JOINED; Genomic_DNA.
DR EMBL; AF159617; AAF19156.1; JOINED; Genomic_DNA.
DR EMBL; AF159618; AAF19156.1; JOINED; Genomic_DNA.
DR EMBL; AF159619; AAF19156.1; JOINED; Genomic_DNA.
DR EMBL; AF159620; AAF19156.1; JOINED; Genomic_DNA.
DR EMBL; AK292181; BAF84870.1; -; mRNA.
DR EMBL; AC090587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471158; EAX02569.1; -; Genomic_DNA.
DR EMBL; CH471158; EAX02568.1; -; Genomic_DNA.
DR EMBL; CH471158; EAX02571.1; -; Genomic_DNA.
DR EMBL; BC009930; AAH09930.1; -; mRNA.
DR EMBL; AL096753; CAB46428.3; -; mRNA.
DR CCDS; CCDS44523.1; -. [Q9UHJ9-5]
DR CCDS; CCDS58112.1; -. [Q9UHJ9-1]
DR CCDS; CCDS58113.1; -. [Q9UHJ9-4]
DR CCDS; CCDS7747.1; -. [Q9UHJ9-2]
DR PIR; T12505; T12505.
DR RefSeq; NP_001138910.1; NM_001145438.2. [Q9UHJ9-5]
DR RefSeq; NP_001243164.1; NM_001256235.1.
DR RefSeq; NP_001243165.1; NM_001256236.1.
DR RefSeq; NP_001243166.1; NM_001256237.1.
DR RefSeq; NP_001243167.1; NM_001256238.1. [Q9UHJ9-4]
DR RefSeq; NP_001243168.1; NM_001256239.1. [Q9UHJ9-3]
DR RefSeq; NP_001243169.1; NM_001256240.1. [Q9UHJ9-1]
DR RefSeq; NP_001269967.1; NM_001283038.1.
DR RefSeq; NP_001269968.1; NM_001283039.1.
DR RefSeq; NP_001269969.1; NM_001283040.1.
DR RefSeq; NP_001333327.1; NM_001346398.1. [Q9UHJ9-1]
DR RefSeq; NP_001333329.1; NM_001346400.1. [Q9UHJ9-3]
DR RefSeq; NP_001333334.1; NM_001346405.1. [Q9UHJ9-1]
DR RefSeq; NP_055304.1; NM_014489.3. [Q9UHJ9-2]
DR RefSeq; XP_006718253.1; XM_006718190.3. [Q9UHJ9-1]
DR RefSeq; XP_006718254.1; XM_006718191.3. [Q9UHJ9-3]
DR RefSeq; XP_011518304.1; XM_011520002.1. [Q9UHJ9-3]
DR RefSeq; XP_011518305.1; XM_011520003.2. [Q9UHJ9-2]
DR RefSeq; XP_011518306.1; XM_011520004.2. [Q9UHJ9-2]
DR AlphaFoldDB; Q9UHJ9; -.
DR BioGRID; 118133; 50.
DR IntAct; Q9UHJ9; 38.
DR TCDB; 9.B.131.1.2; the post-gpi attachment protein (p-gap2) family.
DR iPTMnet; Q9UHJ9; -.
DR PhosphoSitePlus; Q9UHJ9; -.
DR BioMuta; PGAP2; -.
DR DMDM; 544584767; -.
DR EPD; Q9UHJ9; -.
DR MassIVE; Q9UHJ9; -.
DR MaxQB; Q9UHJ9; -.
DR PaxDb; Q9UHJ9; -.
DR PeptideAtlas; Q9UHJ9; -.
DR PRIDE; Q9UHJ9; -.
DR ProteomicsDB; 21134; -.
DR ProteomicsDB; 43326; -.
DR ProteomicsDB; 84365; -. [Q9UHJ9-1]
DR ProteomicsDB; 84366; -. [Q9UHJ9-2]
DR ProteomicsDB; 84367; -. [Q9UHJ9-3]
DR Antibodypedia; 42139; 87 antibodies from 16 providers.
DR DNASU; 27315; -.
DR Ensembl; ENST00000278243.9; ENSP00000278243.4; ENSG00000148985.20. [Q9UHJ9-2]
DR Ensembl; ENST00000300730.10; ENSP00000300730.6; ENSG00000148985.20. [Q9UHJ9-5]
DR Ensembl; ENST00000463452.6; ENSP00000435223.1; ENSG00000148985.20. [Q9UHJ9-1]
DR Ensembl; ENST00000464906.6; ENSP00000434631.2; ENSG00000148985.20. [Q9UHJ9-2]
DR Ensembl; ENST00000493547.6; ENSP00000431851.1; ENSG00000148985.20. [Q9UHJ9-4]
DR GeneID; 27315; -.
DR KEGG; hsa:27315; -.
DR MANE-Select; ENST00000278243.9; ENSP00000278243.4; NM_014489.4; NP_055304.1. [Q9UHJ9-2]
DR UCSC; uc001lys.5; human. [Q9UHJ9-1]
DR CTD; 27315; -.
DR DisGeNET; 27315; -.
DR GeneCards; PGAP2; -.
DR HGNC; HGNC:17893; PGAP2.
DR HPA; ENSG00000148985; Tissue enriched (epididymis).
DR MalaCards; PGAP2; -.
DR MIM; 614207; phenotype.
DR MIM; 615187; gene.
DR neXtProt; NX_Q9UHJ9; -.
DR OpenTargets; ENSG00000148985; -.
DR Orphanet; 247262; Hyperphosphatasia-intellectual disability syndrome.
DR PharmGKB; PA165543520; -.
DR VEuPathDB; HostDB:ENSG00000148985; -.
DR eggNOG; KOG3979; Eukaryota.
DR GeneTree; ENSGT00510000047299; -.
DR InParanoid; Q9UHJ9; -.
DR OMA; HYREHIR; -.
DR OrthoDB; 1166083at2759; -.
DR TreeFam; TF314112; -.
DR PathwayCommons; Q9UHJ9; -.
DR SignaLink; Q9UHJ9; -.
DR BioGRID-ORCS; 27315; 21 hits in 1083 CRISPR screens.
DR ChiTaRS; PGAP2; human.
DR GenomeRNAi; 27315; -.
DR Pharos; Q9UHJ9; Tbio.
DR PRO; PR:Q9UHJ9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UHJ9; protein.
DR Bgee; ENSG00000148985; Expressed in corpus epididymis and 200 other tissues.
DR ExpressionAtlas; Q9UHJ9; baseline and differential.
DR Genevisible; Q9UHJ9; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR039545; PGAP2.
DR PANTHER; PTHR12892; PTHR12892; 1.
DR Pfam; PF10277; Frag1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum;
KW Golgi apparatus; GPI-anchor biosynthesis; Intellectual disability;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Post-GPI attachment to proteins factor 2"
FT /id="PRO_0000326094"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..114
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..185
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..254
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MARLGSTGGVSGRVVTQHRDSAPFLGAPRLGLRELGPIRGTAPEWHG
FT RWNAAERSDKM (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_053800"
FT VAR_SEQ 55
FT /note="G -> GATPCRMFSAASQPLDPDGTLFRLRFTAMVWWAITFPVFGFFFCIIW
FT SLVFHFEYTVATDCG (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10585768,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_032550"
FT VAR_SEQ 172..175
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032551"
FT VAR_SEQ 176..232
FT /note="DRKSYSWKQRLFIINFISFFSALAVYFRHNMYCEAGVYTIFAILEYTVVLTN
FT MAFHM -> VRSIPSGGSKAAQKKIKDICPQDSGSQVLQLETAALHHQLHLLLLGAGCL
FT LSAQHVL (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045984"
FT VAR_SEQ 233..254
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045985"
FT VARIANT 16
FT /note="R -> W (in HPMRS3; dbSNP:rs773359554)"
FT /evidence="ECO:0000269|PubMed:23561847"
FT /id="VAR_069664"
FT VARIANT 99
FT /note="Y -> C (in HPMRS3; dbSNP:rs879255232)"
FT /evidence="ECO:0000269|PubMed:23561846"
FT /id="VAR_069665"
FT VARIANT 127
FT /note="L -> S (in HPMRS3; dbSNP:rs879255233)"
FT /evidence="ECO:0000269|PubMed:23561847"
FT /id="VAR_069666"
FT VARIANT 160
FT /note="T -> I (in HPMRS3; dbSNP:rs780188037)"
FT /evidence="ECO:0000269|PubMed:23561847"
FT /id="VAR_069667"
FT VARIANT 177
FT /note="R -> P (in HPMRS3; dbSNP:rs774843232)"
FT /evidence="ECO:0000269|PubMed:23561846"
FT /id="VAR_069668"
FT CONFLICT 73
FT /note="Q -> H (in Ref. 1; AAF19156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 29400 MW; 2FB502D505DCCF64 CRC64;
MYQVPLPLDR DGTLVRLRFT MVALVTVCCP LVAFLFCILW SLLFHFKETT ATHCGVPNYL
PSVSSAIGGE VPQRYVWRFC IGLHSAPRFL VAFAYWNHYL SCTSPCSCYR PLCRLNFGLN
VVENLALLVL TYVSSSEDFT IHENAFIVFI ASSLGHMLLT CILWRLTKKH TVSQEDRKSY
SWKQRLFIIN FISFFSALAV YFRHNMYCEA GVYTIFAILE YTVVLTNMAF HMTAWWDFGN
KELLITSQPE EKRF
