FRAS1_HUMAN
ID FRAS1_HUMAN Reviewed; 4008 AA.
AC Q86XX4; A2RRR8; Q86UZ4; Q8N3U9; Q8NAU7; Q96JW7; Q9H6N9; Q9P228;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Extracellular matrix organizing protein FRAS1 {ECO:0000250|UniProtKB:Q80T14};
DE AltName: Full=Fraser syndrome 1 protein {ECO:0000303|PubMed:12766769};
DE Flags: Precursor;
GN Name=FRAS1 {ECO:0000312|HGNC:HGNC:19185}; Synonyms=KIAA1500;
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 [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INVOLVEMENT IN FRASRS1.
RX PubMed=12766769; DOI=10.1038/ng1142;
RA McGregor L.K., Makela V., Darling S.M., Vrontou S., Chalepakis G.,
RA Roberts C., Smart N., Rutland P., Prescott N., Hopkins J., Bentley E.,
RA Shaw A., Roberts E., Mueller R., Jadeja S., Philip N., Nelson J.,
RA Francannet C., Perez-Aytes A., Megarbane A., Kerr B., Wainwright B.,
RA Woolf A.S., Winter R.M., Scambler P.J.;
RT "Fraser syndrome and mouse blebbed phenotype caused by mutations in
RT FRAS1/Fras1 encoding a putative extracellular matrix protein.";
RL Nat. Genet. 34:203-208(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 159-4008 (ISOFORM 6).
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-4008 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1560-1953 (ISOFORM 1).
RC TISSUE=Placenta;
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 MRNA] OF 1773-4008 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1773-4008 (ISOFORM 5).
RC TISSUE=Amygdala;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
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 [9]
RP INVOLVEMENT IN FRASRS1.
RX PubMed=23473829; DOI=10.1016/j.gene.2013.02.031;
RA Hoefele J., Wilhelm C., Schiesser M., Mack R., Heinrich U., Weber L.T.,
RA Biskup S., Daumer-Haas C., Klein H.G., Rost I.;
RT "Expanding the mutation spectrum for Fraser syndrome: identification of a
RT novel heterozygous deletion in FRAS1.";
RL Gene 520:194-197(2013).
CC -!- FUNCTION: Involved in extracellular matrix organization (By
CC similarity). Required for the regulation of epidermal-basement membrane
CC adhesion responsible for proper organogenesis during embryonic
CC development (By similarity). Involved in brain organization and
CC function (By similarity). {ECO:0000250|UniProtKB:Q80T14}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80T14};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q80T14};
CC Extracellular side {ECO:0000250|UniProtKB:Q80T14}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86XX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XX4-2; Sequence=VSP_011293, VSP_011294, VSP_011295,
CC VSP_046232, VSP_011299;
CC Name=4;
CC IsoId=Q86XX4-4; Sequence=VSP_011287, VSP_011288;
CC Name=5;
CC IsoId=Q86XX4-5; Sequence=VSP_011291, VSP_011292;
CC Name=6;
CC IsoId=Q86XX4-6; Sequence=VSP_011289, VSP_011290;
CC -!- TISSUE SPECIFICITY: Expressed in many adult tissues, with highest
CC levels in kidney, pancreas and thalamus. Relatively high expression was
CC also detected in fetal kidney and heart. {ECO:0000269|PubMed:12766769}.
CC -!- DOMAIN: The Calx-beta domains bind calcium with high affinity and
CC undergo a major conformational shift upon binding. {ECO:0000250}.
CC -!- DISEASE: Fraser syndrome 1 (FRASRS1) [MIM:219000]: A form of Fraser
CC syndrome, an autosomal recessive disorder characterized by
CC cryptophthalmos, cutaneous syndactyly, and urogenital abnormalities
CC including renal agenesis or hypoplasia. Additional features include
CC abnormalities of the larynx, ear malformations, and facial
CC abnormalities. {ECO:0000269|PubMed:12766769,
CC ECO:0000269|PubMed:23473829}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15216.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ512501; CAD54734.1; -; Genomic_DNA.
DR EMBL; AC093652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052281; AAH52281.1; -; mRNA.
DR EMBL; BC064487; AAH64487.1; -; mRNA.
DR EMBL; BC131820; AAI31821.1; -; mRNA.
DR EMBL; AK025684; BAB15216.1; ALT_FRAME; mRNA.
DR EMBL; AK027833; BAB55399.1; -; mRNA.
DR EMBL; AB040933; BAA96024.2; -; mRNA.
DR EMBL; AL831853; CAD38554.1; -; mRNA.
DR CCDS; CCDS54771.1; -. [Q86XX4-2]
DR CCDS; CCDS54772.1; -. [Q86XX4-5]
DR RefSeq; NP_001159605.1; NM_001166133.1. [Q86XX4-5]
DR RefSeq; NP_079350.5; NM_025074.6. [Q86XX4-2]
DR SMR; Q86XX4; -.
DR BioGRID; 123137; 133.
DR IntAct; Q86XX4; 31.
DR MINT; Q86XX4; -.
DR STRING; 9606.ENSP00000326330; -.
DR GlyGen; Q86XX4; 19 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q86XX4; -.
DR PhosphoSitePlus; Q86XX4; -.
DR SwissPalm; Q86XX4; -.
DR BioMuta; FRAS1; -.
DR DMDM; 476007832; -.
DR EPD; Q86XX4; -.
DR jPOST; Q86XX4; -.
DR MassIVE; Q86XX4; -.
DR MaxQB; Q86XX4; -.
DR PaxDb; Q86XX4; -.
DR PeptideAtlas; Q86XX4; -.
DR PRIDE; Q86XX4; -.
DR ProteomicsDB; 482; -.
DR ProteomicsDB; 70338; -. [Q86XX4-1]
DR ProteomicsDB; 70339; -. [Q86XX4-2]
DR ProteomicsDB; 70340; -. [Q86XX4-4]
DR ProteomicsDB; 70341; -. [Q86XX4-5]
DR ProteomicsDB; 70342; -. [Q86XX4-6]
DR Antibodypedia; 2470; 34 antibodies from 10 providers.
DR DNASU; 80144; -.
DR Ensembl; ENST00000325942.11; ENSP00000326330.6; ENSG00000138759.20. [Q86XX4-5]
DR Ensembl; ENST00000502446.6; ENSP00000423645.2; ENSG00000138759.20. [Q86XX4-4]
DR Ensembl; ENST00000508900.2; ENSP00000423809.2; ENSG00000138759.20. [Q86XX4-6]
DR Ensembl; ENST00000512123.4; ENSP00000422834.2; ENSG00000138759.20. [Q86XX4-2]
DR GeneID; 80144; -.
DR KEGG; hsa:80144; -.
DR MANE-Select; ENST00000512123.4; ENSP00000422834.2; NM_025074.7; NP_079350.5. [Q86XX4-2]
DR UCSC; uc003hkw.4; human. [Q86XX4-1]
DR CTD; 80144; -.
DR DisGeNET; 80144; -.
DR GeneCards; FRAS1; -.
DR HGNC; HGNC:19185; FRAS1.
DR HPA; ENSG00000138759; Tissue enhanced (thyroid).
DR MalaCards; FRAS1; -.
DR MIM; 219000; phenotype.
DR MIM; 607830; gene.
DR neXtProt; NX_Q86XX4; -.
DR OpenTargets; ENSG00000138759; -.
DR Orphanet; 2052; Fraser syndrome.
DR Orphanet; 93100; Renal agenesis, unilateral.
DR PharmGKB; PA134980133; -.
DR VEuPathDB; HostDB:ENSG00000138759; -.
DR eggNOG; KOG1216; Eukaryota.
DR eggNOG; KOG3525; Eukaryota.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000162130; -.
DR HOGENOM; CLU_000898_0_0_1; -.
DR InParanoid; Q86XX4; -.
DR OMA; FTSVNHK; -.
DR OrthoDB; 13258at2759; -.
DR PathwayCommons; Q86XX4; -.
DR SignaLink; Q86XX4; -.
DR BioGRID-ORCS; 80144; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; FRAS1; human.
DR GeneWiki; FRAS1; -.
DR GenomeRNAi; 80144; -.
DR Pharos; Q86XX4; Tbio.
DR PRO; PR:Q86XX4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86XX4; protein.
DR Bgee; ENSG00000138759; Expressed in germinal epithelium of ovary and 142 other tissues.
DR ExpressionAtlas; Q86XX4; baseline and differential.
DR Genevisible; Q86XX4; HS.
DR GO; GO:0005604; C:basement membrane; ISS:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0003338; P:metanephros morphogenesis; IEA:Ensembl.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR CDD; cd00064; FU; 12.
DR Gene3D; 2.60.40.2030; -; 5.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF03160; Calx-beta; 5.
DR Pfam; PF00093; VWC; 4.
DR SMART; SM00237; Calx_beta; 5.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00261; FU; 14.
DR SMART; SM00214; VWC; 6.
DR SMART; SM00215; VWC_out; 3.
DR SUPFAM; SSF141072; SSF141072; 5.
DR SUPFAM; SSF57184; SSF57184; 6.
DR PROSITE; PS51854; CSPG; 12.
DR PROSITE; PS01208; VWFC_1; 6.
DR PROSITE; PS50184; VWFC_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..4008
FT /note="Extracellular matrix organizing protein FRAS1"
FT /id="PRO_0000010120"
FT TOPO_DOM 27..3901
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3902..3922
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3923..4008
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..88
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 93..153
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 157..217
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 219..279
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 283..343
FT /note="VWFC 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 347..417
FT /note="VWFC 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REPEAT 409..460
FT /note="FU 1"
FT REPEAT 462..505
FT /note="FU 2"
FT REPEAT 507..553
FT /note="FU 3"
FT REPEAT 555..599
FT /note="FU 4"
FT REPEAT 602..647
FT /note="FU 5"
FT REPEAT 649..705
FT /note="FU 6"
FT REPEAT 708..753
FT /note="FU 7"
FT REPEAT 755..800
FT /note="FU 8"
FT REPEAT 803..852
FT /note="FU 9"
FT REPEAT 854..900
FT /note="FU 10"
FT REPEAT 903..948
FT /note="FU 11"
FT REPEAT 952..997
FT /note="FU 12"
FT REPEAT 999..1042
FT /note="FU 13"
FT REPEAT 1046..1089
FT /note="FU 14"
FT REPEAT 1102..1197
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1217..1308
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1329..1438
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1463..1559
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1595..1689
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1710..1810
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1833..1936
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1957..2057
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2078..2177
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2199..2291
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2311..2404
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2439..2536
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 2543..2646
FT /note="Calx-beta 1"
FT DOMAIN 2659..2770
FT /note="Calx-beta 2"
FT DOMAIN 2784..2890
FT /note="Calx-beta 3"
FT DOMAIN 2905..3007
FT /note="Calx-beta 4"
FT DOMAIN 3025..3129
FT /note="Calx-beta 5"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1093
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 713..737
FT /note="ACHQSCFRCAGKSPHNCTDCGPSHV -> GQNLDFCQNLEVISAVCLGISST
FT EN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011287"
FT VAR_SEQ 738..4008
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011288"
FT VAR_SEQ 808..809
FT /note="DC -> GE (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011289"
FT VAR_SEQ 810..4008
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011290"
FT VAR_SEQ 1953..1976
FT /note="RKNDEPPRMTLQPLRVQLSSGVVI -> VKTLEVGKVEPLTTIFHTIRELSL
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_011291"
FT VAR_SEQ 1977..4008
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_011292"
FT VAR_SEQ 2156..2157
FT /note="QP -> HV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_011293"
FT VAR_SEQ 2194
FT /note="S -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_011294"
FT VAR_SEQ 2598
FT /note="S -> SSSRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_011295"
FT VAR_SEQ 2717..2718
FT /note="LF -> SL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_046232"
FT VAR_SEQ 3386..3387
FT /note="LA -> IS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_011299"
FT VARIANT 32
FT /note="D -> G (in dbSNP:rs4859905)"
FT /id="VAR_069150"
FT VARIANT 54
FT /note="D -> H (in dbSNP:rs17003071)"
FT /id="VAR_055807"
FT VARIANT 209
FT /note="P -> S (in dbSNP:rs7699637)"
FT /id="VAR_055808"
FT VARIANT 228
FT /note="Y -> H (in dbSNP:rs7682296)"
FT /id="VAR_055809"
FT VARIANT 243
FT /note="I -> V (in dbSNP:rs6848030)"
FT /id="VAR_055810"
FT VARIANT 429
FT /note="S -> Y (in dbSNP:rs6838959)"
FT /id="VAR_055811"
FT VARIANT 466
FT /note="L -> I (in dbSNP:rs12504081)"
FT /id="VAR_055812"
FT VARIANT 590
FT /note="M -> T (in dbSNP:rs35030041)"
FT /id="VAR_055813"
FT VARIANT 687
FT /note="D -> G (in dbSNP:rs345513)"
FT /id="VAR_069151"
FT VARIANT 710
FT /note="I -> L (in dbSNP:rs345512)"
FT /id="VAR_069152"
FT VARIANT 817
FT /note="A -> V (in dbSNP:rs6835769)"
FT /id="VAR_055814"
FT VARIANT 954
FT /note="T -> M (in dbSNP:rs17003166)"
FT /id="VAR_055815"
FT VARIANT 1023
FT /note="G -> E (in dbSNP:rs17459809)"
FT /id="VAR_055816"
FT VARIANT 1136
FT /note="E -> K (in dbSNP:rs12512164)"
FT /id="VAR_055817"
FT VARIANT 1626
FT /note="A -> V (in dbSNP:rs17003213)"
FT /id="VAR_055818"
FT VARIANT 2545
FT /note="D -> N (in dbSNP:rs4388111)"
FT /id="VAR_069153"
SQ SEQUENCE 4008 AA; 443214 MW; 79972020FA59C3CD CRC64;
MGVLKVWLGL ALALAEFAVL PHHSEGACVY QDSLLADATI WKPDSCQSCR CHGDIVICKP
AVCRNPQCAF EKGEVLQIAA NQCCPECVLR TPGSCHHEKK IHEHGTEWAS SPCSVCSCNH
GEVRCTPQPC PPLSCGHQEL AFIPEGSCCP VCVGLGKPCS YEGHVFQDGE DWRLSRCAKC
LCRNGVAQCF TAQCQPLFCN QDETVVRVPG KCCPQCSARS CSAAGQVYEH GEQWSENACT
TCICDRGEVR CHKQACLPLR CGKGQSRARR HGQCCEECVS PAGSCSYDGV VRYQDEMWKG
SACEFCMCDH GQVTCQTGEC AKVECARDEE LIHLDGKCCP ECISRNGYCV YEETGEFMSS
NASEVKRIPE GEKWEDGPCK VCECRGAQVT CYEPSCPPCP VGTLALEVKG QCCPDCTSVH
CHPDCLTCSQ SPDHCDLCQD PTKLLQNGWC VHSCGLGFYQ AGSLCLACQP QCSTCTSGLE
CSSCQPPLLM RHGQCVPTCG DGFYQDRHSC AVCHESCAGC WGPTEKHCLA CRDPLHVLRD
GGCESSCGKG FYNRQGTCSA CDQSCDSCGP SSPRCLTCTE KTVLHDGKCM SECPGGYYAD
ATGRCKVCHN SCASCSGPTP SHCTACSPPK ALRQGHCLPR CGEGFYSDHG VCKACHSSCL
ACMGPAPSHC TGCKKPEEGL QVEQLSDVGI PSGECLAQCR AHFYLESTGI CEACHQSCFR
CAGKSPHNCT DCGPSHVLLD GQCLSQCPDG YFHQEGSCTE CHPTCRQCHG PLESDCISCY
PHISLTNGNC RTSCREEQFL NLVGYCADCH HLCQHCAADL HNTGSICLRC QNAHYLLLGD
HCVPDCPSGY YAERGACKKC HSSCRTCQGR GPFSCSSCDT NLVLSHTGTC STTCFPGHYL
DDNHVCQPCN THCGSCDSQA SCTSCRDPNK VLLFGECQYE SCAPQYYLDF STNTCKECDW
SCSACSGPLK TDCLQCMDGY VLQDGACVEQ CLSSFYQDSG LCKNCDSYCL QCQGPHECTR
CKGPFLLLEA QCVQECGKGY FADHAKHKCT ACPQGCLQCS HRDRCHLCDH GFFLKSGLCV
YNCVPGFSVH TSNETCSGKI HTPSLHVNGS LILPIGSIKP LDFSLLNVQD QEGRVEDLLF
HVVSTPTNGQ LVLSRNGKEV QLDKAGRFSW KDVNEKKVRF VHSKEKLRKG YLFLKISDQQ
FFSEPQLINI QAFSTQAPYV LRNEVLHISR GERATITTQM LDIRDDDNPQ DVVIEIIDPP
LHGQLLQTLQ SPATPIYQFQ LDELSRGLLH YAHDGSDSTS DVAVLQANDG HSFHNILFQV
KTVPQNDRGL QLVANSMVWV PEGGMLQITN RILQAEAPGA SAEEIIYKIT QDYPQFGEVV
LLVNMPADSP ADEGQHLPDG RTATPTSTFT QQDINEGIVW YRHSGAPAQS DSFRFEVSSA
SNAQTRLESH MFNIAILPQT PEAPKVSLEA SLHMTAREDG LTVIQPHSLS FINSEKPSGK
IVYNITLPLH PNQGIIEHRD HPHSPIRYFT QEDINQGKVM YRPPPAAPHL QELMAFSFAG
LPESVKFHFT VSDGEHTSPE MVLTIHLLPS DQQLPVFQVT APRLAVSPGG STSVGLQVVV
RDAETAPKEL FFELRRPPQH GVLLKHTAEF RRPMATGDTF TYEDVEKNAL QYIHDGSSTR
EDSMEISVTD GLTVTMLEVR VEVSLSEDRG PRLAAGSSLS ITVASKSTAI ITRSHLAYVD
DSSPDPEIWI QLNYLPSYGT LLRISGSEVE ELSEVSNFTM EDINNKKIRY SAVFETDGHL
VTDSFYFSVS DMDHNHLDNQ IFTIMITPAE NPPPVIAFAD LITVDEGGRA PLSFHHFFAT
DDDDNLQRDA IIKLSALPKY GCIENTGTGD RFGPETASDL EASFPIQDVL ENYIYYFQSV
HESIEPTHDI FSFYVSDGTS RSEIHSINIT IERKNDEPPR MTLQPLRVQL SSGVVISNSS
LSLQDLDTPD NELIFVLTKK PDHGHVLWRQ TASEPLENGR VLVQGSTFTY QDILAGLVGY
VPSVPGMVVD EFQFSLTDGL HVDTGRMKIY TELPASDTPH LAINQGLQLS AGSVARITEQ
HLKVTDIDSD DHQVMYIMKE DPGAGRLQMM KHGNLEQISI KGPIRSFTQA DISQGQPEYS
HGTGEPGGSF AFKFDVVDGE GNRLIDKSFS ISISEDKSPP VITTNKGLVL DENSVKKITT
LQLSATDQDS GPTELIYRIT RQPQLGHLEH AASPGIQISS FTQADLTSRN VQYVHSSEAE
KHSDAFSFTL SDGVSEVTQT FHITLHPVDD SLPVVQNLGM RVQEGMRKTI TEFELKAVDA
DTEAESVTFT IVQPPRHGTI ERTSNGQHFH LTSTFTMKDI YQNRVSYSHD GSNSLKDRFT
FTVSDGTNPF FIIEEGGKEI MTAAPQPFRV DILPVDDGTP RIVTNLGLQW LEYMDGKATN
LITKKELLTM DPDTEDAQLV YEITTGPKHG FVENKLQPGR AAATFTQEDV NLGLIRYVLH
KEKIREMMDS FQFLVKDSKP NVVSDNVFHI QWSLISFKYT SYNVSEKAGS VSVTVQRTGN
LNQYAIVLCR TEQGTASSSS QPGQQDYVEY AGQVQFDERE DTKSCTIVIN DDDVFENVES
FTVELSMPAY ALLGEFTQAK VIINDTEDEP TLEFDKKIYW VNESAGFLFA PIERKGDASS
IVSAICYTVP KSAMGSLFYA LESGSDFKSR GMSAASRVIF GPGVTMSTCD VMLIDDSEYE
EEEEFEIALA DASDNARIGR VATAKVLISG PNDASTVSLG NTAFTVSEDA GTVKIPVIRH
GTDLSTFASV WCATRPSDPA SATPGVDYVP SSRKVEFGPG VIEQYCTLTI LDDTQYPVIE
GLETFVVFLS SAQGAELTKP FQAVIAINDT FQDVPSMQFA KDLLLVKEKE GVLHVPITRS
GDLSYESSVR CYTQSHSAQV MEDFEERQNA DSSRITFLKG DKVKNCTVYI HDDSMFEPEE
QFRVYLGLPL GNHWSGARIG KNNMATITIS NDEDAPTIEF EEAAYQVREP AGPDAIAILN
IKVIRRGDQN RTSKVRCSTR DGSAQSGVDY YPKSRVLKFS PGVDHIFFKV EILSNEDREW
HESFSLVLGP DDPVEAVLGD VTTATVTILD QEAAGSLILP APPIVVTLAD YDHVEEVTKE
GVKKSPSPGY PLVCVTPCDP HFPRYAVMKE RCSEAGINQT SVQFSWEVAA PTDGNGARSP
FETITDNTPF TSVNHMVLDS IYFSRRFHVR CVAKAVDKVG HVGTPLRSNI VTIGTDSAIC
HTPVVAGTSR GFQAQSFIAT LKYLDVKHKE HPNRIHISVQ IPHQDGMLPL ISTMPLHNLH
FLLSESIYRH QHVCSNLVTT YDLRGLAEAG FLDDVVYDST ALGPGYDRPF QFDPSVREPK
TIQLYKHLNL KSCVWTFDAY YDMTELIDVC GGSVTADFQV RDSAQSFLTV HVPLYVSYIY
VTAPRGWASL EHHTEMEFSF FYDTVLWRTG IQTDSVLSAR LQIIRIYIRE DGRLVIEFKT
HAKFRGQFVM EHHTLPEVKS FVLTPDHLGG IEFDLQLLWS AQTFDSPHQL WRATSSYNRK
DYSGEYTIYL IPCTVQPTQP WVDPGEKPLA CTAHAPERFL IPIAFQQTNR PVPVVYSLNT
EFQLCNNEKV FLMDPNTSDM SLAEMDYKGA FSKGQILYGR VLWNPEQNLN SAYKLQLEKV
YLCTGKDGYV PFFDPTGTIY NEGPQYGCIQ PNKHLKHRFL LLDRNQPEVT DKYFHDVPFE
AHFASELPDF HVVSNMPGVD GFTLKVDALY KVEAGHQWYL QVIYIIGPDT ISGPRVQRSL
TAPLRRNRRD LVEPDGQLIL DDSLIYDNEG DQVKNGTNMK SLNLEMQELA VAASLSQTGA
SIGSALAAIM LLLLVFLVAC FINRKCQKQR KKKPAEDILE EYPLNTKVEV PKRHPDRVEK
NVNRHYCTVR NVNILSEPEA AYTFKGAKVK RLNLEVRVHN NLQDGTEV
