TICN3_HUMAN
ID TICN3_HUMAN Reviewed; 436 AA.
AC Q9BQ16; B2R7M7; B3KR67; B4DGK5; B4DHB4; B4DHV3; B4DI46; B4DJY3; E7EP61;
AC F5H099; O75705; Q6UW53; Q96Q26;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Testican-3;
DE AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3;
DE Flags: Precursor;
GN Name=SPOCK3; Synonyms=TICN3; ORFNames=UNQ409/PRO771;
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 3).
RC TISSUE=Brain;
RA Vannahme C., Hartmann U., Goesling S., Kohfeldt E., Timpl R., Paulsson M.,
RA Maurer P.;
RT "Cloning and expression of testican-3, a novel member of brain-specific,
RT calcium-binding proteoglycans.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION.
RC TISSUE=Fetal kidney;
RX PubMed=11751414;
RA Nakada M., Yamada A., Takino T., Miyamori H., Takahashi T., Yamashita J.,
RA Sato H.;
RT "Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated
RT MMP-2 activation and tumor invasion by testican 3 and its splicing variant
RT gene product, N-Tes.";
RL Cancer Res. 61:8896-8902(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 7), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-356 (ISOFORM 8).
RC TISSUE=Brain, Caudate nucleus, Corpus callosum, and Thalamus;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Muscle;
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).
CC -!- FUNCTION: May participate in diverse steps of neurogenesis. Inhibits
CC the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and
CC MT3-MMP. May interfere with tumor invasion.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=3;
CC IsoId=Q9BQ16-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9BQ16-1; Sequence=VSP_013598;
CC Name=2; Synonyms=N-tes;
CC IsoId=Q9BQ16-2; Sequence=VSP_005334, VSP_005335;
CC Name=4;
CC IsoId=Q9BQ16-4; Sequence=VSP_043681;
CC Name=5;
CC IsoId=Q9BQ16-5; Sequence=VSP_045104;
CC Name=6;
CC IsoId=Q9BQ16-6; Sequence=VSP_045899, VSP_045900;
CC Name=7;
CC IsoId=Q9BQ16-7; Sequence=VSP_046686;
CC Name=8;
CC IsoId=Q9BQ16-8; Sequence=VSP_013598, VSP_046687;
CC Name=9;
CC IsoId=Q9BQ16-9; Sequence=VSP_013598, VSP_005334, VSP_005335;
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- PTM: Contains chondroitin sulfate and heparan sulfate O-linked
CC oligosaccharides. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG58995.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ001454; CAA04775.1; -; mRNA.
DR EMBL; AB056866; BAB64908.1; -; mRNA.
DR EMBL; AY358973; AAQ89332.1; -; mRNA.
DR EMBL; AK091078; BAG52279.1; -; mRNA.
DR EMBL; AK295281; BAG58265.1; -; mRNA.
DR EMBL; AK295407; BAG58358.1; -; mRNA.
DR EMBL; AK294637; BAG57816.1; -; mRNA.
DR EMBL; AK295015; BAG58075.1; -; mRNA.
DR EMBL; AK296291; BAG58995.1; ALT_INIT; mRNA.
DR EMBL; AK313042; BAG35874.1; -; mRNA.
DR EMBL; AC010103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04811.1; -; Genomic_DNA.
DR EMBL; BC000460; AAH00460.1; -; mRNA.
DR EMBL; BC003017; AAH03017.1; -; mRNA.
DR EMBL; BC013983; AAH13983.1; -; mRNA.
DR CCDS; CCDS34095.1; -. [Q9BQ16-1]
DR CCDS; CCDS54817.1; -. [Q9BQ16-3]
DR CCDS; CCDS56343.1; -. [Q9BQ16-7]
DR CCDS; CCDS56344.1; -. [Q9BQ16-4]
DR CCDS; CCDS56346.1; -. [Q9BQ16-8]
DR CCDS; CCDS56347.1; -. [Q9BQ16-9]
DR CCDS; CCDS58931.1; -. [Q9BQ16-5]
DR RefSeq; NP_001035249.1; NM_001040159.1. [Q9BQ16-1]
DR RefSeq; NP_001191281.1; NM_001204352.1. [Q9BQ16-4]
DR RefSeq; NP_001191282.1; NM_001204353.1. [Q9BQ16-7]
DR RefSeq; NP_001191283.1; NM_001204354.1.
DR RefSeq; NP_001191284.1; NM_001204355.1. [Q9BQ16-6]
DR RefSeq; NP_001191285.1; NM_001204356.1. [Q9BQ16-8]
DR RefSeq; NP_001191287.1; NM_001204358.1. [Q9BQ16-9]
DR RefSeq; NP_001238896.1; NM_001251967.1. [Q9BQ16-5]
DR RefSeq; NP_058646.2; NM_016950.2. [Q9BQ16-3]
DR RefSeq; XP_011530320.1; XM_011532018.1. [Q9BQ16-3]
DR RefSeq; XP_016863747.1; XM_017008258.1. [Q9BQ16-1]
DR AlphaFoldDB; Q9BQ16; -.
DR SMR; Q9BQ16; -.
DR BioGRID; 119160; 5.
DR IntAct; Q9BQ16; 4.
DR MINT; Q9BQ16; -.
DR STRING; 9606.ENSP00000349677; -.
DR MEROPS; I01.980; -.
DR MEROPS; I31.007; -.
DR GlyGen; Q9BQ16; 2 sites.
DR iPTMnet; Q9BQ16; -.
DR PhosphoSitePlus; Q9BQ16; -.
DR BioMuta; SPOCK3; -.
DR DMDM; 67473703; -.
DR jPOST; Q9BQ16; -.
DR MassIVE; Q9BQ16; -.
DR MaxQB; Q9BQ16; -.
DR PaxDb; Q9BQ16; -.
DR PeptideAtlas; Q9BQ16; -.
DR PRIDE; Q9BQ16; -.
DR ProteomicsDB; 17290; -.
DR ProteomicsDB; 25277; -.
DR ProteomicsDB; 4139; -.
DR ProteomicsDB; 4275; -.
DR ProteomicsDB; 4419; -.
DR ProteomicsDB; 78611; -. [Q9BQ16-3]
DR ProteomicsDB; 78612; -. [Q9BQ16-1]
DR ProteomicsDB; 78613; -. [Q9BQ16-2]
DR ProteomicsDB; 78614; -. [Q9BQ16-4]
DR TopDownProteomics; Q9BQ16-2; -. [Q9BQ16-2]
DR TopDownProteomics; Q9BQ16-3; -. [Q9BQ16-3]
DR TopDownProteomics; Q9BQ16-5; -. [Q9BQ16-5]
DR Antibodypedia; 28345; 133 antibodies from 19 providers.
DR DNASU; 50859; -.
DR Ensembl; ENST00000357154.7; ENSP00000349677.3; ENSG00000196104.11. [Q9BQ16-3]
DR Ensembl; ENST00000357545.9; ENSP00000350153.4; ENSG00000196104.11. [Q9BQ16-1]
DR Ensembl; ENST00000421836.6; ENSP00000411344.2; ENSG00000196104.11. [Q9BQ16-4]
DR Ensembl; ENST00000502330.5; ENSP00000423606.1; ENSG00000196104.11. [Q9BQ16-3]
DR Ensembl; ENST00000504953.5; ENSP00000425570.1; ENSG00000196104.11. [Q9BQ16-1]
DR Ensembl; ENST00000506886.5; ENSP00000420920.1; ENSG00000196104.11. [Q9BQ16-3]
DR Ensembl; ENST00000510741.5; ENSP00000426716.1; ENSG00000196104.11. [Q9BQ16-8]
DR Ensembl; ENST00000511269.5; ENSP00000425502.1; ENSG00000196104.11. [Q9BQ16-1]
DR Ensembl; ENST00000511531.5; ENSP00000423421.1; ENSG00000196104.11. [Q9BQ16-3]
DR Ensembl; ENST00000512648.5; ENSP00000426177.1; ENSG00000196104.11. [Q9BQ16-9]
DR Ensembl; ENST00000512681.5; ENSP00000426318.1; ENSG00000196104.11. [Q9BQ16-5]
DR Ensembl; ENST00000541354.5; ENSP00000444789.1; ENSG00000196104.11. [Q9BQ16-7]
DR GeneID; 50859; -.
DR KEGG; hsa:50859; -.
DR MANE-Select; ENST00000357545.9; ENSP00000350153.4; NM_001040159.2; NP_001035249.1. [Q9BQ16-1]
DR UCSC; uc003iri.2; human. [Q9BQ16-3]
DR CTD; 50859; -.
DR DisGeNET; 50859; -.
DR GeneCards; SPOCK3; -.
DR HGNC; HGNC:13565; SPOCK3.
DR HPA; ENSG00000196104; Tissue enhanced (brain, parathyroid gland, prostate).
DR MIM; 607989; gene.
DR neXtProt; NX_Q9BQ16; -.
DR OpenTargets; ENSG00000196104; -.
DR PharmGKB; PA134977377; -.
DR VEuPathDB; HostDB:ENSG00000196104; -.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000157828; -.
DR HOGENOM; CLU_037217_1_0_1; -.
DR InParanoid; Q9BQ16; -.
DR OMA; LDKNEHC; -.
DR OrthoDB; 1235834at2759; -.
DR PhylomeDB; Q9BQ16; -.
DR TreeFam; TF317779; -.
DR PathwayCommons; Q9BQ16; -.
DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR SignaLink; Q9BQ16; -.
DR BioGRID-ORCS; 50859; 14 hits in 1060 CRISPR screens.
DR ChiTaRS; SPOCK3; human.
DR GenomeRNAi; 50859; -.
DR Pharos; Q9BQ16; Tbio.
DR PRO; PR:Q9BQ16; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BQ16; protein.
DR Bgee; ENSG00000196104; Expressed in lateral globus pallidus and 155 other tissues.
DR ExpressionAtlas; Q9BQ16; baseline and differential.
DR Genevisible; Q9BQ16; HS.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; TAS:ParkinsonsUK-UCL.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparan sulfate; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..436
FT /note="Testican-3"
FT /id="PRO_0000026703"
FT DOMAIN 133..185
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 314..380
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 393..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 387
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..111
FT /evidence="ECO:0000250"
FT DISULFID 139..169
FT /evidence="ECO:0000250"
FT DISULFID 142..162
FT /evidence="ECO:0000250"
FT DISULFID 151..183
FT /evidence="ECO:0000250"
FT DISULFID 317..341
FT /evidence="ECO:0000250"
FT DISULFID 352..359
FT /evidence="ECO:0000250"
FT DISULFID 361..380
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046686"
FT VAR_SEQ 1..66
FT /note="MLKVSAVLCVCAAAWCSQSLAAAAAVAAAGGRSDGGNFLDDKQWLTTISQYD
FT KEVGQWNKFRDEVE -> MITQDHIHMSSGLSQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043681"
FT VAR_SEQ 1..24
FT /note="MLKVSAVLCVCAAAWCSQSLAAAA -> MINNGSPQSLSMTRKSDSGTNSET
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045899"
FT VAR_SEQ 25..120
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045900"
FT VAR_SEQ 64..161
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045104"
FT VAR_SEQ 64..66
FT /note="Missing (in isoform 1, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013598"
FT VAR_SEQ 200..240
FT /note="ACSDLEFREVANRLRDWFKALHESGSQNKKTKTLLRPERSR -> G (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046687"
FT VAR_SEQ 314..316
FT /note="DPP -> GKR (in isoform 2 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11751414"
FT /id="VSP_005334"
FT VAR_SEQ 317..436
FT /note="Missing (in isoform 2 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11751414"
FT /id="VSP_005335"
FT VARIANT 112
FT /note="I -> V (in dbSNP:rs9685645)"
FT /id="VAR_051562"
FT CONFLICT 348
FT /note="K -> M (in Ref. 1; CAA04775)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="E -> G (in Ref. 4; BAG58265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 49429 MW; AAEDD1998C656FC0 CRC64;
MLKVSAVLCV CAAAWCSQSL AAAAAVAAAG GRSDGGNFLD DKQWLTTISQ YDKEVGQWNK
FRDEVEDDYF RTWSPGKPFD QALDPAKDPC LKMKCSRHKV CIAQDSQTAV CISHRRLTHR
MKEAGVDHRQ WRGPILSTCK QCPVVYPSPV CGSDGHTYSF QCKLEYQACV LGKQISVKCE
GHCPCPSDKP TSTSRNVKRA CSDLEFREVA NRLRDWFKAL HESGSQNKKT KTLLRPERSR
FDTSILPICK DSLGWMFNRL DTNYDLLLDQ SELRSIYLDK NEQCTKAFFN SCDTYKDSLI
SNNEWCYCFQ RQQDPPCQTE LSNIQKRQGV KKLLGQYIPL CDEDGYYKPT QCHGSVGQCW
CVDRYGNEVM GSRINGVADC AIDFEISGDF ASGDFHEWTD DEDDEDDIMN DEDEIEDDDE
DEGDDDDGGD DHDVYI
