ID   PPBI_HUMAN              Reviewed;         528 AA.
AC   P09923; B2R7Y4; Q53S80; Q9UBV5; Q9UCL2;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Intestinal-type alkaline phosphatase;
DE            Short=IAP;
DE            Short=Intestinal alkaline phosphatase;
DE            EC=3.1.3.1;
DE   Flags: Precursor;
GN   Name=ALPI;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3468508; DOI=10.1073/pnas.84.3.695;
RA   Berger J., Garattini E., Hua J.-C., Udenfriend S.;
RT   "Cloning and sequencing of human intestinal alkaline phosphatase cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:695-698(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3469665; DOI=10.1073/pnas.84.5.1234;
RA   Henthorn P.S., Raducha M., Edwards Y.H., Weiss M.J., Slaughter C.,
RA   Lafferty M.A., Harris H.;
RT   "Nucleotide and amino acid sequences of human intestinal alkaline
RT   phosphatase: close homology to placental alkaline phosphatase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:1234-1238(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2841341; DOI=10.1016/s0021-9258(18)37886-4;
RA   Henthorn P.S., Raducha M., Kadesch T., Weiss M.J., Harris H.;
RT   "Sequence and characterization of the human intestinal alkaline phosphatase
RT   gene.";
RL   J. Biol. Chem. 263:12011-12019(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=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   [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].
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 [GENOMIC DNA] OF 1-100.
RX   PubMed=3697102; DOI=10.1093/nar/15.24.10599;
RA   Millan J.L.;
RT   "Promoter structure of the human intestinal alkaline phosphatase gene.";
RL   Nucleic Acids Res. 15:10599-10599(1987).
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   PROTEIN SEQUENCE OF 20-58.
RX   PubMed=3458202; DOI=10.1073/pnas.83.8.2368;
RA   Hua J.-C., Berger J., Pan Y.C.E., Hulmes J.D., Udenfriend S.;
RT   "Partial sequencing of human adult, human fetal, and bovine intestinal
RT   alkaline phosphatases: comparison with the human placental and liver
RT   isozymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:2368-2372(1986).
RN   [11]
RP   PROTEIN SEQUENCE OF 20-49.
RX   PubMed=1458595;
RA   Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T., Hirano K.;
RT   "Chemical nature of intestinal-type alkaline phosphatase in human kidney.";
RL   Clin. Chem. 38:2539-2542(1992).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
CC   -!- FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate
CC       compounds. {ECO:0000250|UniProtKB:P15693}.
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:0000250|UniProtKB:P15693, ECO:0000255|PROSITE-
CC         ProRule:PRU10042};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P15693};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P15693};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P15693};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P15693};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P05186};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15693}.
CC   -!- INTERACTION:
CC       P09923; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1052631, EBI-10171774;
CC       P09923; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1052631, EBI-10172052;
CC       P09923; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-1052631, EBI-945833;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15693};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15693}.
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).
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
CC       URL="https://en.wikipedia.org/wiki/Alkaline_phosphatase";
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DR   EMBL; M15694; AAA51703.1; -; mRNA.
DR   EMBL; M31008; AAA51704.1; -; mRNA.
DR   EMBL; J03930; AAA98617.1; -; Genomic_DNA.
DR   EMBL; AK313163; BAG35981.1; -; mRNA.
DR   EMBL; AC068134; AAY24089.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70997.1; -; Genomic_DNA.
DR   EMBL; BC132678; AAI32679.1; -; mRNA.
DR   EMBL; Y00512; CAA68564.1; -; Genomic_DNA.
DR   EMBL; M19161; AAA51705.1; -; Genomic_DNA.
DR   CCDS; CCDS2492.1; -.
DR   PIR; A31073; PAHUI.
DR   RefSeq; NP_001622.2; NM_001631.4.
DR   AlphaFoldDB; P09923; -.
DR   SMR; P09923; -.
DR   BioGRID; 106749; 89.
DR   IntAct; P09923; 22.
DR   MINT; P09923; -.
DR   STRING; 9606.ENSP00000295463; -.
DR   BindingDB; P09923; -.
DR   ChEMBL; CHEMBL5573; -.
DR   DrugBank; DB12816; Terpinen-4-ol.
DR   DrugBank; DB16349; Vicagrel.
DR   DEPOD; ALPI; -.
DR   GlyConnect; 11; 9 N-Linked glycans.
DR   GlyCosmos; P09923; 3 sites, 17 glycans.
DR   GlyGen; P09923; 4 sites, 17 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P09923; -.
DR   PhosphoSitePlus; P09923; -.
DR   BioMuta; ALPI; -.
DR   DMDM; 130744; -.
DR   EPD; P09923; -.
DR   jPOST; P09923; -.
DR   MassIVE; P09923; -.
DR   MaxQB; P09923; -.
DR   PaxDb; 9606-ENSP00000295463; -.
DR   PeptideAtlas; P09923; -.
DR   ProteomicsDB; 52281; -.
DR   Antibodypedia; 20217; 831 antibodies from 34 providers.
DR   DNASU; 248; -.
DR   Ensembl; ENST00000295463.4; ENSP00000295463.3; ENSG00000163295.5.
DR   GeneID; 248; -.
DR   KEGG; hsa:248; -.
DR   MANE-Select; ENST00000295463.4; ENSP00000295463.3; NM_001631.5; NP_001622.2.
DR   UCSC; uc002vst.4; human.
DR   AGR; HGNC:437; -.
DR   CTD; 248; -.
DR   DisGeNET; 248; -.
DR   GeneCards; ALPI; -.
DR   HGNC; HGNC:437; ALPI.
DR   HPA; ENSG00000163295; Tissue enriched (intestine).
DR   MIM; 171740; gene.
DR   neXtProt; NX_P09923; -.
DR   OpenTargets; ENSG00000163295; -.
DR   PharmGKB; PA24728; -.
DR   VEuPathDB; HostDB:ENSG00000163295; -.
DR   eggNOG; KOG4126; Eukaryota.
DR   GeneTree; ENSGT00950000183063; -.
DR   HOGENOM; CLU_008539_4_0_1; -.
DR   InParanoid; P09923; -.
DR   OMA; HEGLAYH; -.
DR   OrthoDB; 35876at2759; -.
DR   PhylomeDB; P09923; -.
DR   TreeFam; TF323513; -.
DR   PathwayCommons; P09923; -.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   Reactome; R-HSA-8935690; Digestion.
DR   SABIO-RK; P09923; -.
DR   SignaLink; P09923; -.
DR   BioGRID-ORCS; 248; 12 hits in 1161 CRISPR screens.
DR   ChiTaRS; ALPI; human.
DR   GeneWiki; ALPI; -.
DR   GenomeRNAi; 248; -.
DR   Pharos; P09923; Tchem.
DR   PRO; PR:P09923; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P09923; Protein.
DR   Bgee; ENSG00000163295; Expressed in jejunal mucosa and 27 other cell types or tissues.
DR   ExpressionAtlas; P09923; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004035; F:alkaline phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF30; INTESTINAL-TYPE ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
DR   Genevisible; P09923; HS.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:1458595,
FT                   ECO:0000269|PubMed:3458202"
FT   CHAIN           20..503
FT                   /note="Intestinal-type alkaline phosphatase"
FT                   /id="PRO_0000024037"
FT   PROPEP          504..528
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024038"
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:P15693"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
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:P15693"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   BINDING         451
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
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   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        140..202
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   DISULFID        486..493
FT                   /evidence="ECO:0000250|UniProtKB:P15693"
FT   VARIANT         144
FT                   /note="R -> H (in dbSNP:rs7559279)"
FT                   /id="VAR_050524"
FT   VARIANT         298
FT                   /note="H -> L (in dbSNP:rs1047223)"
FT                   /id="VAR_011816"
FT   CONFLICT        347
FT                   /note="L -> V (in Ref. 2; AAA51703)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        410
FT                   /note="I -> T (in Ref. 1; AAA51704)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="P -> L (in Ref. 2; AAA51703)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   528 AA;  56812 MW;  465306BEDF9F0B79 CRC64;
     MQGPWVLLLL GLRLQLSLGV IPAEEENPAF WNRQAAEALD AAKKLQPIQK VAKNLILFLG
     DGLGVPTVTA TRILKGQKNG KLGPETPLAM DRFPYLALSK TYNVDRQVPD SAATATAYLC
     GVKANFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKQAGK SVGVVTTTRV QHASPAGTYA
     HTVNRNWYSD ADMPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPADA
     SQNGIRLDGK NLVQEWLAKH QGAWYVWNRT ELMQASLDQS VTHLMGLFEP GDTKYEIHRD
     PTLDPSLMEM TEAALRLLSR NPRGFYLFVE GGRIDHGHHE GVAYQALTEA VMFDDAIERA
     GQLTSEEDTL TLVTADHSHV FSFGGYTLRG SSIFGLAPSK AQDSKAYTSI LYGNGPGYVF
     NSGVRPDVNE SESGSPDYQQ QAAVPLSSET HGGEDVAVFA RGPQAHLVHG VQEQSFVAHV
     MAFAACLEPY TACDLAPPAC TTDAAHPVAA SLPLLAGTLL LLGASAAP
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