NPTN_HUMAN
ID NPTN_HUMAN Reviewed; 398 AA.
AC Q9Y639; B2RAL7; B7Z4D3; B7ZLL2; Q17R52; Q59EJ9; Q6NVX7; Q9Y640;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Neuroplastin;
DE AltName: Full=Stromal cell-derived receptor 1;
DE Short=SDR-1;
DE Flags: Precursor;
GN Name=NPTN; Synonyms=SDFR1, SDR1;
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] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
RA Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T.,
RA Tashiro K., Honjo T.;
RT "Isoform specific expression of the SDR-1 protein, alpha and beta in
RT subregions of adult rodent brain.";
RL Biomed. Res. 20:43-49(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain, and Stomach;
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 MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 29-43 (ISOFORM 1).
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17196182; DOI=10.1016/j.brainres.2006.11.090;
RA Bernstein H.G., Smalla K.H., Bogerts B., Gordon-Weeks P.R., Beesley P.W.,
RA Gundelfinger E.D., Kreutz M.R.;
RT "The immunolocalization of the synaptic glycoprotein neuroplastin differs
RT substantially between the human and the rodent brain.";
RL Brain Res. 1134:107-112(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-284 AND ASN-296.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-229.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH XKR8.
RX PubMed=27503893; DOI=10.1073/pnas.1610403113;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Xkr8 phospholipid scrambling complex in apoptotic phosphatidylserine
RT exposure.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9509-9514(2016).
RN [12] {ECO:0007744|PDB:6A69}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS) IN COMPLEX WITH ATP2B1,
RP FUNCTION, TOPOLOGY, AND DISULFIDE BOND.
RX PubMed=30190470; DOI=10.1038/s41467-018-06075-7;
RA Gong D., Chi X., Ren K., Huang G., Zhou G., Yan N., Lei J., Zhou Q.;
RT "Structure of the human plasma membrane Ca2+-ATPase 1 in complex with its
RT obligatory subunit neuroplastin.";
RL Nat. Commun. 9:3623-3623(2018).
CC -!- FUNCTION: Probable homophilic and heterophilic cell adhesion molecule
CC involved in long term potentiation at hippocampal excitatory synapses
CC through activation of p38MAPK. May also regulate neurite outgrowth by
CC activating the FGFR1 signaling pathway. May play a role in synaptic
CC plasticity (By similarity). Also acts as a chaperone for ATP2B1;
CC stabilizes ATP2B1 and increases its ATPase activity (PubMed:30190470).
CC Promotes localization of XKR8 at the cell membrane (PubMed:27503893).
CC {ECO:0000250|UniProtKB:P97546, ECO:0000269|PubMed:27503893,
CC ECO:0000269|PubMed:30190470}.
CC -!- SUBUNIT: Interacts with ATP2B1; this interaction stabilizes ATP2B1 and
CC increases ATPase activity; this interaction controls T cell calcium
CC homeostasis following T cell activation (PubMed:30190470). Interacts
CC with XKR8; promoting its localization at the cell membrane
CC (PubMed:27503893). {ECO:0000269|PubMed:27503893,
CC ECO:0000269|PubMed:30190470}.
CC -!- INTERACTION:
CC Q9Y639-1; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12839590, EBI-3867333;
CC Q9Y639-1; P42858: HTT; NbExp=6; IntAct=EBI-12839590, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97546};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P97546}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Postsynaptic density
CC {ECO:0000250|UniProtKB:P97546}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2; Synonyms=SDR-1-beta;
CC IsoId=Q9Y639-2; Sequence=Displayed;
CC Name=1; Synonyms=SDR-1-alpha;
CC IsoId=Q9Y639-1; Sequence=VSP_039251;
CC Name=3;
CC IsoId=Q9Y639-3; Sequence=VSP_039251, VSP_039253;
CC Name=4;
CC IsoId=Q9Y639-4; Sequence=VSP_039252;
CC Name=5;
CC IsoId=Q9Y639-5; Sequence=VSP_039253;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is
CC expressed in brain cortex and cerebellum (at protein level).
CC {ECO:0000269|PubMed:17196182, ECO:0000269|Ref.1}.
CC -!- DOMAIN: Some isoforms lack the first Ig-like domain which may confer
CC homophilic adhesion activity. However, they can bind and activate FGFR1
CC (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93049.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF109126; AAD43217.1; -; mRNA.
DR EMBL; AF109127; AAD43218.1; -; mRNA.
DR EMBL; AK297184; BAH12519.1; -; mRNA.
DR EMBL; AK314248; BAG36914.1; -; mRNA.
DR EMBL; AB209812; BAD93049.1; ALT_INIT; mRNA.
DR EMBL; CH471082; EAW77931.1; -; Genomic_DNA.
DR EMBL; BC105979; AAI05980.1; -; mRNA.
DR EMBL; BC117462; AAI17463.1; -; mRNA.
DR EMBL; BC143880; AAI43881.1; -; mRNA.
DR EMBL; BC143881; AAI43882.1; -; mRNA.
DR CCDS; CCDS10249.1; -. [Q9Y639-2]
DR CCDS; CCDS10250.1; -. [Q9Y639-1]
DR CCDS; CCDS58379.1; -. [Q9Y639-3]
DR CCDS; CCDS58380.1; -. [Q9Y639-5]
DR PIR; T17219; T17219.
DR RefSeq; NP_001154835.1; NM_001161363.1. [Q9Y639-5]
DR RefSeq; NP_001154836.1; NM_001161364.1. [Q9Y639-3]
DR RefSeq; NP_036560.1; NM_012428.3. [Q9Y639-2]
DR RefSeq; NP_059429.1; NM_017455.3. [Q9Y639-1]
DR PDB; 6A69; EM; 4.11 A; B=146-398.
DR PDBsum; 6A69; -.
DR AlphaFoldDB; Q9Y639; -.
DR SMR; Q9Y639; -.
DR BioGRID; 117958; 259.
DR IntAct; Q9Y639; 8.
DR MINT; Q9Y639; -.
DR STRING; 9606.ENSP00000290401; -.
DR TCDB; 8.A.23.1.8; the basigin (basigin) family.
DR GlyConnect; 1558; 7 N-Linked glycans (2 sites).
DR GlyGen; Q9Y639; 7 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; Q9Y639; -.
DR PhosphoSitePlus; Q9Y639; -.
DR BioMuta; NPTN; -.
DR DMDM; 298286871; -.
DR EPD; Q9Y639; -.
DR jPOST; Q9Y639; -.
DR MassIVE; Q9Y639; -.
DR MaxQB; Q9Y639; -.
DR PaxDb; Q9Y639; -.
DR PeptideAtlas; Q9Y639; -.
DR PRIDE; Q9Y639; -.
DR ProteomicsDB; 86593; -. [Q9Y639-2]
DR ProteomicsDB; 86594; -. [Q9Y639-1]
DR ProteomicsDB; 86595; -. [Q9Y639-3]
DR ProteomicsDB; 86596; -. [Q9Y639-4]
DR ProteomicsDB; 86597; -. [Q9Y639-5]
DR Antibodypedia; 26797; 343 antibodies from 27 providers.
DR DNASU; 27020; -.
DR Ensembl; ENST00000345330.9; ENSP00000290401.4; ENSG00000156642.17. [Q9Y639-2]
DR Ensembl; ENST00000351217.10; ENSP00000342958.6; ENSG00000156642.17. [Q9Y639-1]
DR Ensembl; ENST00000562924.5; ENSP00000456349.1; ENSG00000156642.17. [Q9Y639-3]
DR Ensembl; ENST00000563691.5; ENSP00000457028.1; ENSG00000156642.17. [Q9Y639-5]
DR GeneID; 27020; -.
DR KEGG; hsa:27020; -.
DR MANE-Select; ENST00000345330.9; ENSP00000290401.4; NM_012428.4; NP_036560.1.
DR UCSC; uc002avr.4; human. [Q9Y639-2]
DR CTD; 27020; -.
DR DisGeNET; 27020; -.
DR GeneCards; NPTN; -.
DR HGNC; HGNC:17867; NPTN.
DR HPA; ENSG00000156642; Low tissue specificity.
DR MIM; 612820; gene.
DR neXtProt; NX_Q9Y639; -.
DR OpenTargets; ENSG00000156642; -.
DR PharmGKB; PA134927704; -.
DR VEuPathDB; HostDB:ENSG00000156642; -.
DR eggNOG; ENOG502QPKN; Eukaryota.
DR GeneTree; ENSGT00940000156195; -.
DR HOGENOM; CLU_058449_0_0_1; -.
DR InParanoid; Q9Y639; -.
DR OMA; HPTWTWH; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; Q9Y639; -.
DR TreeFam; TF326759; -.
DR PathwayCommons; Q9Y639; -.
DR Reactome; R-HSA-977443; GABA receptor activation.
DR SignaLink; Q9Y639; -.
DR BioGRID-ORCS; 27020; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; NPTN; human.
DR GeneWiki; NPTN; -.
DR GenomeRNAi; 27020; -.
DR Pharos; Q9Y639; Tbio.
DR PRO; PR:Q9Y639; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y639; protein.
DR Bgee; ENSG00000156642; Expressed in Brodmann (1909) area 23 and 209 other tissues.
DR ExpressionAtlas; Q9Y639; baseline and differential.
DR Genevisible; Q9Y639; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; ISS:HGNC-UCL.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:HGNC-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:1904861; P:excitatory synapse assembly; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISS:HGNC-UCL.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1903829; P:positive regulation of protein localization; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1902683; P:regulation of receptor localization to synapse; IEA:Ensembl.
DR GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR027112; Neuroplastin.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF5; PTHR10075:SF5; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT CHAIN 29..398
FT /note="Neuroplastin"
FT /id="PRO_0000394470"
FT TOPO_DOM 29..339
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30190470"
FT TOPO_DOM 361..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..134
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 148..235
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 238..329
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 149..161
FT /note="Narpin; mediates binding with FGFR1 and has
FT antidepressant-like activity"
FT /evidence="ECO:0000250"
FT REGION 365..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..316
FT /evidence="ECO:0000269|PubMed:30190470"
FT VAR_SEQ 31..147
FT /note="AGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGA
FT RKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQAT
FT ISVLQK -> E (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_039251"
FT VAR_SEQ 320..398
FT /note="NAIGSASVVTVLRVRSHLAPLWPFLGILAEIIILVVIIVVYEKRKRPDEVPD
FT DDEPAGPMKTNSTNNHKDKNLRQRNTN -> WPHSGLSWEFWLKLSSLW (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_039252"
FT VAR_SEQ 372..375
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_039253"
FT CONFLICT 299
FT /note="E -> K (in Ref. 2; BAH12519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44387 MW; 5109E3C03B4967EA CRC64;
MSGSSLPSAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL YCDVVGSPTP
EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV LRITRLTLED SGTYECRASN
DPKRNDLRQN PSITWIRAQA TISVLQKPRI VTSEEVIIRD SPVLPVTLQC NLTSSSHTLT
YSYWTKNGVE LSATRKNASN MEYRINKPRA EDSGEYHCVY HFVSAPKANA TIEVKAAPDI
TGHKRSENKN EGQDATMYCK SVGYPHPDWI WRKKENGMPM DIVNTSGRFF IINKENYTEL
NIVNLQITED PGEYECNATN AIGSASVVTV LRVRSHLAPL WPFLGILAEI IILVVIIVVY
EKRKRPDEVP DDDEPAGPMK TNSTNNHKDK NLRQRNTN
