NPNT_HUMAN
ID NPNT_HUMAN Reviewed; 565 AA.
AC Q6UXI9; A6NFT9; A8K1W4; B4DIT4; B4DYK3; B4E2H7; B4E3H2; D6RCA1; E9PCK8;
AC E9PCQ1; E9PE64; E9PF04;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nephronectin;
DE AltName: Full=Preosteoblast EGF-like repeat protein with MAM domain;
DE AltName: Full=Protein EGFL6-like;
DE Flags: Precursor;
GN Name=NPNT; Synonyms=EGFL6L, POEM; ORFNames=UNQ295/PRO334;
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 2), AND VARIANTS HIS-159
RP AND VAL-234.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4; 5 AND 6), AND
RP VARIANT VAL-234.
RC TISSUE=Hippocampus, Testis, Trachea, and 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-234.
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 [5]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15754038;
RA Huang J.T.-J., Lee V.;
RT "Identification and characterization of a novel human nephronectin gene in
RT silico.";
RL Int. J. Mol. Med. 15:719-724(2005).
CC -!- FUNCTION: Functional ligand of integrin alpha-8/beta-1 in kidney
CC development. Regulates the expression of GDNF with integrin alpha-
CC 8/beta-1 which is essential for kidney development. May also play a
CC role in the development and function of various tissues, regulating
CC cell adhesion, spreading and survival through the binding of several
CC integrins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Note=Trapped on the cell surface or in the
CC extracellular matrix. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q6UXI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UXI9-2; Sequence=VSP_026987, VSP_026988;
CC Name=3;
CC IsoId=Q6UXI9-3; Sequence=VSP_045813;
CC Name=4;
CC IsoId=Q6UXI9-4; Sequence=VSP_045813, VSP_026987;
CC Name=5;
CC IsoId=Q6UXI9-5; Sequence=VSP_026987;
CC Name=6;
CC IsoId=Q6UXI9-6; Sequence=VSP_046131;
CC -!- TISSUE SPECIFICITY: Expressed in kidney and lung and to a lower extent
CC in brain, pregnant uterus, placenta, thyroid gland and blood vessels.
CC {ECO:0000269|PubMed:15754038}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal kidney, cochlea, eye, heart and
CC lung. {ECO:0000269|PubMed:15754038}.
CC -!- DOMAIN: The MAM domain is required for localization at the cell
CC surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
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DR EMBL; AY358336; AAQ88702.1; -; mRNA.
DR EMBL; AK290029; BAF82718.1; -; mRNA.
DR EMBL; AK295772; BAG58596.1; -; mRNA.
DR EMBL; AK302477; BAG63765.1; -; mRNA.
DR EMBL; AK304279; BAG65139.1; -; mRNA.
DR EMBL; AK304721; BAG65484.1; -; mRNA.
DR EMBL; AC093782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06196.1; -; Genomic_DNA.
DR CCDS; CCDS34046.1; -. [Q6UXI9-1]
DR CCDS; CCDS54784.1; -. [Q6UXI9-6]
DR CCDS; CCDS54785.1; -. [Q6UXI9-3]
DR CCDS; CCDS54786.1; -. [Q6UXI9-4]
DR CCDS; CCDS54787.1; -. [Q6UXI9-5]
DR RefSeq; NP_001028219.1; NM_001033047.2. [Q6UXI9-1]
DR RefSeq; NP_001171619.1; NM_001184690.1. [Q6UXI9-6]
DR RefSeq; NP_001171620.1; NM_001184691.1. [Q6UXI9-3]
DR RefSeq; NP_001171621.1; NM_001184692.1. [Q6UXI9-5]
DR RefSeq; NP_001171622.1; NM_001184693.1. [Q6UXI9-4]
DR AlphaFoldDB; Q6UXI9; -.
DR SMR; Q6UXI9; -.
DR BioGRID; 129117; 10.
DR STRING; 9606.ENSP00000389252; -.
DR GlyConnect; 1540; 13 N-Linked glycans (1 site).
DR GlyGen; Q6UXI9; 4 sites, 12 N-linked glycans (1 site), 3 O-linked glycans (3 sites).
DR iPTMnet; Q6UXI9; -.
DR PhosphoSitePlus; Q6UXI9; -.
DR BioMuta; NPNT; -.
DR DMDM; 311033424; -.
DR jPOST; Q6UXI9; -.
DR MassIVE; Q6UXI9; -.
DR PeptideAtlas; Q6UXI9; -.
DR PRIDE; Q6UXI9; -.
DR ProteomicsDB; 19464; -.
DR ProteomicsDB; 19490; -.
DR ProteomicsDB; 19819; -.
DR ProteomicsDB; 19996; -.
DR ProteomicsDB; 67631; -. [Q6UXI9-1]
DR ProteomicsDB; 67632; -. [Q6UXI9-2]
DR Antibodypedia; 1021; 130 antibodies from 22 providers.
DR DNASU; 255743; -.
DR Ensembl; ENST00000305572.12; ENSP00000302557.8; ENSG00000168743.13. [Q6UXI9-2]
DR Ensembl; ENST00000379987.7; ENSP00000369323.2; ENSG00000168743.13. [Q6UXI9-1]
DR Ensembl; ENST00000427316.6; ENSP00000389252.2; ENSG00000168743.13. [Q6UXI9-3]
DR Ensembl; ENST00000453617.6; ENSP00000402884.2; ENSG00000168743.13. [Q6UXI9-6]
DR Ensembl; ENST00000506666.5; ENSP00000422474.1; ENSG00000168743.13. [Q6UXI9-4]
DR Ensembl; ENST00000514622.5; ENSP00000422044.1; ENSG00000168743.13. [Q6UXI9-5]
DR GeneID; 255743; -.
DR KEGG; hsa:255743; -.
DR MANE-Select; ENST00000379987.7; ENSP00000369323.2; NM_001033047.3; NP_001028219.1.
DR UCSC; uc003hya.4; human. [Q6UXI9-1]
DR CTD; 255743; -.
DR DisGeNET; 255743; -.
DR GeneCards; NPNT; -.
DR HGNC; HGNC:27405; NPNT.
DR HPA; ENSG00000168743; Tissue enhanced (lung, thyroid gland).
DR MIM; 610306; gene.
DR neXtProt; NX_Q6UXI9; -.
DR OpenTargets; ENSG00000168743; -.
DR VEuPathDB; HostDB:ENSG00000168743; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00930000150973; -.
DR HOGENOM; CLU_036867_0_0_1; -.
DR InParanoid; Q6UXI9; -.
DR OMA; GKTCNQG; -.
DR OrthoDB; 766075at2759; -.
DR PhylomeDB; Q6UXI9; -.
DR TreeFam; TF330819; -.
DR PathwayCommons; Q6UXI9; -.
DR SignaLink; Q6UXI9; -.
DR SIGNOR; Q6UXI9; -.
DR BioGRID-ORCS; 255743; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; NPNT; human.
DR GenomeRNAi; 255743; -.
DR Pharos; Q6UXI9; Tbio.
DR PRO; PR:Q6UXI9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6UXI9; protein.
DR Bgee; ENSG00000168743; Expressed in right lobe of thyroid gland and 164 other tissues.
DR ExpressionAtlas; Q6UXI9; baseline and differential.
DR Genevisible; Q6UXI9; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030485; C:smooth muscle contractile fiber; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; ISS:BHF-UCL.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:BHF-UCL.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISS:BHF-UCL.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:BHF-UCL.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:BHF-UCL.
DR GO; GO:0097195; P:pilomotor reflex; IEA:Ensembl.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:BHF-UCL.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; ISS:BHF-UCL.
DR CDD; cd06263; MAM; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..565
FT /note="Nephronectin"
FT /id="PRO_0000295684"
FT DOMAIN 52..87
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 89..128
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..168
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 169..213
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..254
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 420..563
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 301..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 382..384
FT /note="Integrin interaction"
FT COMPBIAS 315..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 56..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 60..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 93..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 115..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 173..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 180..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 197..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 58
FT /note="P -> PFYVLRQRIARIRCQLKA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046131"
FT VAR_SEQ 88
FT /note="Q -> QDEHIPAPLDQGSEQPLFQPLDHQATSLPSR (in isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045813"
FT VAR_SEQ 387..416
FT /note="IPRQPSNDLFEIFEIERGVSADDEAKDDPG -> S (in isoform 2,
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_026987"
FT VAR_SEQ 535..564
FT /note="VVFKGEKRRGHTGEIGLDDVSLKKGHCSEE -> ESQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_026988"
FT VARIANT 159
FT /note="Q -> H (in dbSNP:rs35132891)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_033314"
FT VARIANT 234
FT /note="I -> V (in dbSNP:rs4340795)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_033315"
FT VARIANT 473
FT /note="G -> S (in dbSNP:rs35613262)"
FT /id="VAR_033316"
FT VARIANT 476
FT /note="M -> T (in dbSNP:rs35488797)"
FT /id="VAR_033317"
FT CONFLICT 20
FT /note="E -> K (in Ref. 2; BAG63765)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="T -> A (in Ref. 2; BAG65139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 61907 MW; D4AB4C41B7D5A819 CRC64;
MDFLLALVLV SSLYLQAAAE FDGRWPRQIV SSIGLCRYGG RIDCCWGWAR QSWGQCQPVC
QPRCKHGECI GPNKCKCHPG YAGKTCNQDL NECGLKPRPC KHRCMNTYGS YKCYCLNGYM
LMPDGSCSSA LTCSMANCQY GCDVVKGQIR CQCPSPGLQL APDGRTCVDV DECATGRASC
PRFRQCVNTF GSYICKCHKG FDLMYIGGKY QCHDIDECSL GQYQCSSFAR CYNIRGSYKC
KCKEGYQGDG LTCVYIPKVM IEPSGPIHVP KGNGTILKGD TGNNNWIPDV GSTWWPPKTP
YIPPIITNRP TSKPTTRPTP KPTPIPTPPP PPPLPTELRT PLPPTTPERP TTGLTTIAPA
ASTPPGGITV DNRVQTDPQK PRGDVFIPRQ PSNDLFEIFE IERGVSADDE AKDDPGVLVH
SCNFDHGLCG WIREKDNDLH WEPIRDPAGG QYLTVSAAKA PGGKAARLVL PLGRLMHSGD
LCLSFRHKVT GLHSGTLQVF VRKHGAHGAA LWGRNGGHGW RQTQITLRGA DIKSVVFKGE
KRRGHTGEIG LDDVSLKKGH CSEER
