ID   ITM2C_HUMAN             Reviewed;         267 AA.
AC   Q9NQX7; B3KPG4; Q4G0A8; Q53H84; Q6IAE7; Q86VK5; Q8N288; Q8TAW0; Q9BUP8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Integral membrane protein 2C;
DE   AltName: Full=Cerebral protein 14;
DE   AltName: Full=Transmembrane protein BRI3;
DE   Contains:
DE     RecName: Full=CT-BRI3;
GN   Name=ITM2C; Synonyms=BRI3; ORFNames=hucep-14, NPD018, PSEC0047;
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] (ISOFORM 1), AND VARIANT SER-53.
RC   TISSUE=Brain;
RA   Yoshimoto M., Yazaki M., Matsumoto K., Takayama K.;
RT   "Molecular cloning of a gene specifically expressed in human brain.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=11290423; DOI=10.1016/s0378-1119(01)00374-2;
RA   Vidal R., Calero M., Revesz T., Plant G., Ghiso J., Frangione B.;
RT   "Sequence, genomic structure and tissue expression of human BRI3, a member
RT   of the BRI gene family.";
RL   Gene 266:95-102(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Wu J., Zhang B., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pituitary;
RA   Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   SER-53.
RC   TISSUE=Amygdala;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-53.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Teratocarcinoma;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-53.
RC   TISSUE=Uterus;
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   [11]
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   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP   SER-53.
RC   TISSUE=Brain, Chondrosarcoma, and Colon;
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   [13]
RP   INTERACTION WITH BACE1, GLYCOSYLATION, CLEAVAGE, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF 241-LYS-ARG-242.
RX   PubMed=15606899; DOI=10.1111/j.1471-4159.2004.02840.x;
RA   Wickham L., Benjannet S., Marcinkiewicz E., Chretien M., Seidah N.G.;
RT   "Beta-amyloid protein converting enzyme 1 and brain-specific type II
RT   membrane protein BRI3: binding partners processed by furin.";
RL   J. Neurochem. 92:93-102(2005).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH STMN2.
RX   PubMed=18452648; DOI=10.5483/bmbrep.2008.41.4.287;
RA   Gong Y., Wu J., Qiang H., Liu B., Chi Z., Chen T., Yin B., Peng X.,
RA   Yuan J.;
RT   "BRI3 associates with SCG10 and attenuates NGF-induced neurite outgrowth in
RT   PC12 cells.";
RL   BMB Rep. 41:287-293(2008).
RN   [15]
RP   ABSENCE OF CLEAVAGE BY ADAM10 AND SPPL2B, AND SUBCELLULAR LOCATION.
RX   PubMed=19114711; DOI=10.1074/jbc.m807485200;
RA   Martin L., Fluhrer R., Haass C.;
RT   "Substrate requirements for SPPL2b-dependent regulated intramembrane
RT   proteolysis.";
RL   J. Biol. Chem. 284:5662-5670(2009).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH APP.
RX   PubMed=19366692; DOI=10.1074/jbc.m109.006403;
RA   Matsuda S., Matsuda Y., D'Adamio L.;
RT   "BRI3 inhibits amyloid precursor protein processing in a mechanistically
RT   distinct manner from its homologue dementia gene BRI2.";
RL   J. Biol. Chem. 284:15815-15825(2009).
RN   [17]
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).
CC   -!- FUNCTION: Negative regulator of amyloid-beta peptide production. May
CC       inhibit the processing of APP by blocking its access to alpha- and
CC       beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal
CC       fragment is negligible, suggesting that ITM2C is a poor gamma-secretase
CC       cleavage inhibitor. May play a role in TNF-induced cell death and
CC       neuronal differentiation (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:18452648, ECO:0000269|PubMed:19366692}.
CC   -!- SUBUNIT: Interacts with BACE1. Interacts with APP. Interacts with
CC       STMN2. {ECO:0000269|PubMed:15606899, ECO:0000269|PubMed:18452648,
CC       ECO:0000269|PubMed:19366692}.
CC   -!- INTERACTION:
CC       Q9NQX7-3; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-12811565, EBI-10271156;
CC       Q9NQX7-3; Q07325: CXCL9; NbExp=3; IntAct=EBI-12811565, EBI-3911467;
CC       Q9NQX7-3; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12811565, EBI-12142257;
CC       Q9NQX7-3; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-12811565, EBI-2804156;
CC       Q9NQX7-3; O00526: UPK2; NbExp=3; IntAct=EBI-12811565, EBI-10179682;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Cell membrane
CC       {ECO:0000269|PubMed:19114711}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:19114711}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9NQX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQX7-2; Sequence=VSP_013471;
CC       Name=3;
CC         IsoId=Q9NQX7-3; Sequence=VSP_013472;
CC   -!- TISSUE SPECIFICITY: High levels in the brain, specifically in the
CC       cerebral cortex, medulla, amygdala, hippocampus, thalamus, caudate
CC       nucleus, cerebellum, olfactory lobe and spinal cord. Very low levels in
CC       other organs. {ECO:0000269|PubMed:11290423,
CC       ECO:0000269|PubMed:15606899}.
CC   -!- PTM: Type I membrane-bound, as well as soluble, furin has a pre-eminent
CC       role in ITM2C proteolytic processing. PCSK7 and PCSK5 may also be
CC       involved although to a lesser extent. The soluble form of PCSK7 is
CC       incapable of processing ITM2C. Fails to undergo shedding by ADAM10 and
CC       intramembrane cleavage by SPPL2B. {ECO:0000269|PubMed:15606899}.
CC   -!- SIMILARITY: Belongs to the ITM2 family. {ECO:0000305}.
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DR   EMBL; AB003629; BAB46927.1; -; mRNA.
DR   EMBL; AF272043; AAF89492.1; -; mRNA.
DR   EMBL; AY049777; AAL15434.1; -; mRNA.
DR   EMBL; AF271781; AAG44792.1; -; mRNA.
DR   EMBL; AL136603; CAB66538.1; -; mRNA.
DR   EMBL; AK056321; BAG51676.1; -; mRNA.
DR   EMBL; AK090975; BAC03562.1; -; mRNA.
DR   EMBL; CR457208; CAG33489.1; -; mRNA.
DR   EMBL; AK222697; BAD96417.1; -; mRNA.
DR   EMBL; AK075361; BAC11570.1; -; mRNA.
DR   EMBL; AL713651; CAD28460.1; -; mRNA.
DR   EMBL; CH471063; EAW70936.1; -; Genomic_DNA.
DR   EMBL; BC002424; AAH02424.1; -; mRNA.
DR   EMBL; BC025742; AAH25742.1; -; mRNA.
DR   EMBL; BC050668; AAH50668.1; -; mRNA.
DR   EMBL; BC098563; AAH98563.1; -; mRNA.
DR   CCDS; CCDS2479.1; -. [Q9NQX7-1]
DR   CCDS; CCDS33395.1; -. [Q9NQX7-3]
DR   CCDS; CCDS33396.1; -. [Q9NQX7-2]
DR   RefSeq; NP_001012532.1; NM_001012514.2. [Q9NQX7-2]
DR   RefSeq; NP_001012534.1; NM_001012516.2. [Q9NQX7-3]
DR   RefSeq; NP_001274169.1; NM_001287240.1.
DR   RefSeq; NP_001274170.1; NM_001287241.1. [Q9NQX7-1]
DR   RefSeq; NP_112188.1; NM_030926.5. [Q9NQX7-1]
DR   AlphaFoldDB; Q9NQX7; -.
DR   BioGRID; 123553; 111.
DR   IntAct; Q9NQX7; 31.
DR   MINT; Q9NQX7; -.
DR   STRING; 9606.ENSP00000322730; -.
DR   TCDB; 1.C.81.2.3; the arenicin (arenicin) family.
DR   GlyCosmos; Q9NQX7; 1 site, No reported glycans.
DR   GlyGen; Q9NQX7; 1 site.
DR   iPTMnet; Q9NQX7; -.
DR   PhosphoSitePlus; Q9NQX7; -.
DR   SwissPalm; Q9NQX7; -.
DR   BioMuta; ITM2C; -.
DR   DMDM; 12585259; -.
DR   EPD; Q9NQX7; -.
DR   jPOST; Q9NQX7; -.
DR   MassIVE; Q9NQX7; -.
DR   MaxQB; Q9NQX7; -.
DR   PaxDb; 9606-ENSP00000322730; -.
DR   PeptideAtlas; Q9NQX7; -.
DR   ProteomicsDB; 82226; -. [Q9NQX7-1]
DR   ProteomicsDB; 82227; -. [Q9NQX7-2]
DR   ProteomicsDB; 82228; -. [Q9NQX7-3]
DR   Pumba; Q9NQX7; -.
DR   Antibodypedia; 34409; 173 antibodies from 20 providers.
DR   DNASU; 81618; -.
DR   Ensembl; ENST00000326407.10; ENSP00000322100.6; ENSG00000135916.16. [Q9NQX7-3]
DR   Ensembl; ENST00000326427.11; ENSP00000322730.6; ENSG00000135916.16. [Q9NQX7-1]
DR   Ensembl; ENST00000335005.10; ENSP00000335121.6; ENSG00000135916.16. [Q9NQX7-2]
DR   GeneID; 81618; -.
DR   KEGG; hsa:81618; -.
DR   MANE-Select; ENST00000326427.11; ENSP00000322730.6; NM_030926.6; NP_112188.1.
DR   UCSC; uc002vqz.5; human. [Q9NQX7-1]
DR   AGR; HGNC:6175; -.
DR   CTD; 81618; -.
DR   DisGeNET; 81618; -.
DR   GeneCards; ITM2C; -.
DR   HGNC; HGNC:6175; ITM2C.
DR   HPA; ENSG00000135916; Tissue enhanced (brain, intestine).
DR   MIM; 609554; gene.
DR   neXtProt; NX_Q9NQX7; -.
DR   OpenTargets; ENSG00000135916; -.
DR   PharmGKB; PA29972; -.
DR   VEuPathDB; HostDB:ENSG00000135916; -.
DR   eggNOG; KOG4681; Eukaryota.
DR   GeneTree; ENSGT00950000183115; -.
DR   InParanoid; Q9NQX7; -.
DR   OMA; AGNCNHI; -.
DR   OrthoDB; 3664639at2759; -.
DR   PhylomeDB; Q9NQX7; -.
DR   TreeFam; TF317770; -.
DR   PathwayCommons; Q9NQX7; -.
DR   SignaLink; Q9NQX7; -.
DR   BioGRID-ORCS; 81618; 10 hits in 1158 CRISPR screens.
DR   ChiTaRS; ITM2C; human.
DR   GeneWiki; ITM2C; -.
DR   GenomeRNAi; 81618; -.
DR   Pharos; Q9NQX7; Tbio.
DR   PRO; PR:Q9NQX7; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9NQX7; Protein.
DR   Bgee; ENSG00000135916; Expressed in mucosa of transverse colon and 196 other cell types or tissues.
DR   ExpressionAtlas; Q9NQX7; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0001540; F:amyloid-beta binding; IPI:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR   GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   Gene3D; 3.30.390.150; -; 1.
DR   InterPro; IPR007084; BRICHOS_dom.
DR   InterPro; IPR040145; ITM2.
DR   PANTHER; PTHR10962:SF5; INTEGRAL MEMBRANE PROTEIN 2C; 1.
DR   PANTHER; PTHR10962; INTEGRAL TRANSMEMBRANE PROTEIN 2; 1.
DR   Pfam; PF04089; BRICHOS; 1.
DR   SMART; SM01039; BRICHOS; 1.
DR   PROSITE; PS50869; BRICHOS; 1.
DR   Genevisible; Q9NQX7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..267
FT                   /note="Integral membrane protein 2C"
FT                   /id="PRO_0000154826"
FT   PEPTIDE         243..267
FT                   /note="CT-BRI3"
FT                   /id="PRO_0000232645"
FT   TRANSMEM        55..75
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          136..230
FT                   /note="BRICHOS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT   SITE            242..243
FT                   /note="Cleavage; by furin"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQL7"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:15606899"
FT   DISULFID        163..222
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         41..87
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013471"
FT   VAR_SEQ         151..187
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013472"
FT   VARIANT         53
FT                   /note="G -> S (in dbSNP:rs2289235)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|Ref.1, ECO:0000269|Ref.7"
FT                   /id="VAR_022111"
FT   MUTAGEN         241..242
FT                   /note="KR->AA: Completely abrogates proteolytic
FT                   processing."
FT                   /evidence="ECO:0000269|PubMed:15606899"
FT   CONFLICT        22..39
FT                   /note="Missing (in Ref. 6; BAC03562)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="V -> A (in Ref. 8; BAD96417)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="T -> A (in Ref. 7; CAG33489)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  30224 MW;  234DDB91B4F282E7 CRC64;
     MVKISFQPAV AGIKGDKADK ASASAPAPAS ATEILLTPAR EEQPPQHRSK RGGSVGGVCY
     LSMGMVVLLM GLVFASVYIY RYFFLAQLAR DNFFRCGVLY EDSLSSQVRT QMELEEDVKI
     YLDENYERIN VPVPQFGGGD PADIIHDFQR GLTAYHDISL DKCYVIELNT TIVLPPRNFW
     ELLMNVKRGT YLPQTYIIQE EMVVTEHVSD KEALGSFIYH LCNGKDTYRL RRRATRRRIN
     KRGAKNCNAI RHFENTFVVE TLICGVV
//