PPBN_HUMAN
ID PPBN_HUMAN Reviewed; 532 AA.
AC P10696; A8KAF2; Q16727; Q53S81; Q96CM1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Alkaline phosphatase, germ cell type {ECO:0000305};
DE EC=3.1.3.1 {ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000269|PubMed:1939159};
DE AltName: Full=ALP-1;
DE AltName: Full=Alkaline phosphatase Nagao isozyme;
DE AltName: Full=Alkaline phosphatase, placental-like;
DE AltName: Full=Germ cell alkaline phosphatase {ECO:0000303|PubMed:1939159};
DE Short=GCAP {ECO:0000303|PubMed:1939159};
DE AltName: Full=Placental alkaline phosphatase-like;
DE Short=PLAP-like;
DE Flags: Precursor;
GN Name=ALPG {ECO:0000312|HGNC:HGNC:441};
GN Synonyms=ALPPL, ALPPL2 {ECO:0000312|HGNC:HGNC:441};
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].
RX PubMed=2834730; DOI=10.1073/pnas.85.9.3024;
RA Millan J.L., Manes T.;
RT "Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline
RT phosphatase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3024-3028(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Choriocarcinoma;
RX PubMed=2745460; DOI=10.1016/s0021-9258(18)63900-6;
RA Watanabe S., Watanabe T., Li W.L., Soong B.-W., Chou J.Y.;
RT "Expression of the germ cell alkaline phosphatase gene in human
RT choriocarcinoma cells.";
RL J. Biol. Chem. 264:12611-12619(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MET-273 AND ARG-316.
RC TISSUE=Colon;
RX PubMed=2297757;
RA Gum J.R. Jr., Hicks J.W., Sack T.L., Kim Y.S.;
RT "Molecular cloning of complementary DNAs encoding alkaline phosphatase in
RT human colon cancer cells.";
RL Cancer Res. 50:1085-1091(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-316.
RX PubMed=2162249;
RA Lowe M.E., Strauss A.W.;
RT "Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline
RT phosphatase in human choriocarcinomas.";
RL Cancer Res. 50:3956-3962(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-316.
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-316.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-273 AND ARG-316.
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RX PubMed=3443302; DOI=10.1016/0378-1119(87)90235-6;
RA Knoll B.J., Rothblum K.N., Longley M.;
RT "Two gene duplication events in the evolution of the human heat-stable
RT alkaline phosphatases.";
RL Gene 60:267-276(1987).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
RX PubMed=3387245; DOI=10.1093/nar/16.12.5694;
RA Shen L.P., Liu H., Kan Y.W., Kam W.;
RT "5' nucleotide sequence of a putative human placental alkaline phosphatase-
RT like gene.";
RL Nucleic Acids Res. 16:5694-5694(1988).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=1939159; DOI=10.1016/s0021-9258(18)54836-5;
RA Watanabe T., Wada N., Kim E.E., Wyckoff H.W., Chou J.Y.;
RT "Mutation of a single amino acid converts germ cell alkaline phosphatase to
RT placental alkaline phosphatase.";
RL J. Biol. Chem. 266:21174-21178(1991).
CC -!- FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate
CC compounds. {ECO:0000269|PubMed:1939159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10042,
CC ECO:0000269|PubMed:1939159};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P05187};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P05187};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P05186};
CC -!- ACTIVITY REGULATION: Inhibited by L-leucine, EDTA and heat.
CC {ECO:0000269|PubMed:1939159}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05187}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Trace amounts in the testis and thymus, and in
CC elevated amounts in germ cell tumors.
CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
CC placental (ALPP), germ cell (ALPG), intestinal (ALPI) and tissue non-
CC specific (liver/bone/kidney) (ALPL/TNAP). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30232.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J03252; AAA98616.1; -; Genomic_DNA.
DR EMBL; J04948; AAA51700.1; -; mRNA.
DR EMBL; X53279; CAA37374.1; -; mRNA.
DR EMBL; X55958; CAA39425.1; -; mRNA.
DR EMBL; AK293017; BAF85706.1; -; mRNA.
DR EMBL; AC068134; AAY24088.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70994.1; -; Genomic_DNA.
DR EMBL; BC014139; AAH14139.1; -; mRNA.
DR EMBL; M19160; AAA51707.1; -; Genomic_DNA.
DR EMBL; X07247; CAA30232.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS2491.1; -.
DR PIR; S12076; S12076.
DR RefSeq; NP_112603.2; NM_031313.2.
DR AlphaFoldDB; P10696; -.
DR SMR; P10696; -.
DR BioGRID; 106752; 41.
DR IntAct; P10696; 12.
DR STRING; 9606.ENSP00000295453; -.
DR BindingDB; P10696; -.
DR ChEMBL; CHEMBL3402; -.
DR DrugBank; DB01143; Amifostine.
DR DrugBank; DB11091; Hydrogen peroxide.
DR DrugBank; DB00848; Levamisole.
DR DrugBank; DB09498; Strontium chloride Sr-89.
DR DEPOD; ALPG; -.
DR GlyGen; P10696; 2 sites.
DR iPTMnet; P10696; -.
DR PhosphoSitePlus; P10696; -.
DR BioMuta; ALPPL2; -.
DR DMDM; 145559564; -.
DR EPD; P10696; -.
DR jPOST; P10696; -.
DR MassIVE; P10696; -.
DR MaxQB; P10696; -.
DR PaxDb; P10696; -.
DR PeptideAtlas; P10696; -.
DR PRIDE; P10696; -.
DR ProteomicsDB; 52638; -.
DR Antibodypedia; 20216; 219 antibodies from 30 providers.
DR DNASU; 251; -.
DR Ensembl; ENST00000295453.8; ENSP00000295453.3; ENSG00000163286.9.
DR GeneID; 251; -.
DR KEGG; hsa:251; -.
DR MANE-Select; ENST00000295453.8; ENSP00000295453.3; NM_031313.3; NP_112603.2.
DR UCSC; uc002vss.5; human.
DR CTD; 251; -.
DR DisGeNET; 251; -.
DR GeneCards; ALPG; -.
DR HGNC; HGNC:441; ALPG.
DR HPA; ENSG00000163286; Not detected.
DR MIM; 171810; gene.
DR neXtProt; NX_P10696; -.
DR OpenTargets; ENSG00000163286; -.
DR PharmGKB; PA24731; -.
DR VEuPathDB; HostDB:ENSG00000163286; -.
DR eggNOG; KOG4126; Eukaryota.
DR GeneTree; ENSGT00950000183063; -.
DR InParanoid; P10696; -.
DR OMA; QPGEMAY; -.
DR OrthoDB; 454880at2759; -.
DR PhylomeDB; P10696; -.
DR TreeFam; TF323513; -.
DR PathwayCommons; P10696; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; P10696; -.
DR BioGRID-ORCS; 251; 6 hits in 999 CRISPR screens.
DR GenomeRNAi; 251; -.
DR Pharos; P10696; Tchem.
DR PRO; PR:P10696; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P10696; protein.
DR Bgee; ENSG00000163286; Expressed in colonic mucosa and 20 other tissues.
DR Genevisible; P10696; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:HGNC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..503
FT /note="Alkaline phosphatase, germ cell type"
FT /id="PRO_0000024033"
FT PROPEP 504..532
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024034"
FT REGION 422..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT LIPID 503
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..202
FT /evidence="ECO:0000250"
FT DISULFID 486..493
FT /evidence="ECO:0000250"
FT VARIANT 273
FT /note="L -> M (in dbSNP:rs17416141)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2297757"
FT /id="VAR_027553"
FT VARIANT 316
FT /note="L -> R (in dbSNP:rs183793479)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2162249,
FT ECO:0000269|PubMed:2297757, ECO:0000269|Ref.7"
FT /id="VAR_027554"
FT VARIANT 527
FT /note="G -> E (in dbSNP:rs1048999)"
FT /id="VAR_027555"
FT CONFLICT 57
FT /note="I -> M (in Ref. 1; AAA98616)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="M -> V (in Ref. 1; AAA98616 and 4; CAA39425)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="A -> T (in Ref. 1; AAA98616, 2; AAA51700 and 4;
FT CAA39425)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="H -> R (in Ref. 8; AAH14139)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="V -> L (in Ref. 2; AAA51700)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> P (in Ref. 1; AAA98616 and 4; CAA39425)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> S (in Ref. 3; CAA37374)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="A -> T (in Ref. 3; CAA37374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 57377 MW; 25EB56C901B61505 CRC64;
MQGPWVLLLL GLRLQLSLGI IPVEEENPDF WNRQAAEALG AAKKLQPAQT AAKNLIIFLG
DGMGVSTVTA ARILKGQKKD KLGPETFLAM DRFPYVALSK TYSVDKHVPD SGATATAYLC
GVKGNFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKKAGK SVGVVTTTRV QHASPAGAYA
HTVNRNWYSD ADVPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPDDY
SQGGTRLDGK NLVQEWLAKH QGARYVWNRT ELLQASLDPS VTHLMGLFEP GDMKYEIHRD
STLDPSLMEM TEAALLLLSR NPRGFFLFVE GGRIDHGHHE SRAYRALTET IMFDDAIERA
GQLTSEEDTL SLVTADHSHV FSFGGYPLRG SSIFGLAPGK ARDRKAYTVL LYGNGPGYVL
KDGARPDVTE SESGSPEYRQ QSAVPLDGET HAGEDVAVFA RGPQAHLVHG VQEQTFIAHV
MAFAACLEPY TACDLAPRAG TTDAAHPGPS VVPALLPLLA GTLLLLGTAT AP
