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 27-MAR-2024, entry version 192. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7. DR IntAct; Q9BQ16; 4. DR MINT; Q9BQ16; -. DR STRING; 9606.ENSP00000349677; -. DR MEROPS; I01.980; -. DR MEROPS; I31.007; -. DR GlyCosmos; Q9BQ16; 2 sites, No reported glycans. DR GlyGen; Q9BQ16; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9BQ16; -. DR PhosphoSitePlus; Q9BQ16; -. DR BioMuta; SPOCK3; -. DR DMDM; 67473703; -. DR jPOST; Q9BQ16; -. DR MassIVE; Q9BQ16; -. DR MaxQB; Q9BQ16; -. DR PaxDb; 9606-ENSP00000349677; -. DR PeptideAtlas; 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; 156 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 AGR; HGNC:13565; -. 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; PQTAVCI; -. DR OrthoDB; 4174283at2759; -. 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 1138 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 157 other cell types or tissues. DR ExpressionAtlas; Q9BQ16; baseline and differential. 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 CDD; cd16239; EFh_SPARC_TICN3; 1. DR CDD; cd00104; KAZAL_FS; 1. DR CDD; cd00191; TY; 1. DR Gene3D; 3.30.60.30; -; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 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 PANTHER; PTHR13866; SPARC OSTEONECTIN; 1. DR PANTHER; PTHR13866:SF21; TESTICAN-3; 1. 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; SSF47473; EF-hand; 1. DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1. DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1. DR PROSITE; PS51465; KAZAL_2; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1. DR Genevisible; Q9BQ16; HS. 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 //