FREM1_HUMAN
ID FREM1_HUMAN Reviewed; 2179 AA.
AC Q5H8C1; B7ZBX4; Q5VV00; Q5VV01; Q6MZI4; Q8NEG9; Q96LI3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=FRAS1-related extracellular matrix protein 1 {ECO:0000305};
DE AltName: Full=Protein QBRICK;
DE Flags: Precursor;
GN Name=FREM1 {ECO:0000312|HGNC:HGNC:23399};
GN Synonyms=C9orf143, C9orf145, C9orf154;
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 VARIANTS LEU-439; VAL-863 AND
RP PRO-2143.
RX PubMed=15878328; DOI=10.1016/j.yexcr.2005.01.020;
RA Kiyozumi D., Osada A., Sugimoto N., Weber C.N., Ono Y., Imai T., Okada A.,
RA Sekiguchi K.;
RT "Identification of a novel cell-adhesive protein spatiotemporally expressed
RT in the basement membrane of mouse developing hair follicle.";
RL Exp. Cell Res. 306:9-23(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 3).
RC TISSUE=Fetal kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS PRO-2143
RP AND GLY-2174.
RC TISSUE=Testis;
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 INTERACTION WITH FREM2.
RX PubMed=29688405; DOI=10.1093/hmg/ddy144;
RA Yu Q., Lin B., Xie S., Gao S., Li W., Liu Y., Wang H., Huang D., Xie Z.;
RT "A homozygous mutation p.Arg2167Trp in FREM2 causes isolated
RT cryptophthalmos.";
RL Hum. Mol. Genet. 27:2357-2366(2018).
RN [7]
RP VARIANTS BNAR TRP-649 AND SER-1440.
RX PubMed=19732862; DOI=10.1016/j.ajhg.2009.08.010;
RA Alazami A.M., Shaheen R., Alzahrani F., Snape K., Saggar A., Brinkmann B.,
RA Bavi P., Al-Gazali L.I., Alkuraya F.S.;
RT "FREM1 mutations cause bifid nose, renal agenesis, and anorectal
RT malformations syndrome.";
RL Am. J. Hum. Genet. 85:414-418(2009).
RN [8]
RP VARIANTS MOTA ARG-1324 AND ILE-2091.
RX PubMed=21507892; DOI=10.1136/jmg.2011.089631;
RA Slavotinek A.M., Baranzini S.E., Schanze D., Labelle-Dumais C., Short K.M.,
RA Chao R., Yahyavi M., Bijlsma E.K., Chu C., Musone S., Wheatley A.,
RA Kwok P.Y., Marles S., Fryns J.P., Maga A.M., Hassan M.G., Gould D.B.,
RA Madireddy L., Li C., Cox T.C., Smyth I., Chudley A.E., Zenker M.;
RT "Manitoba-oculo-tricho-anal (MOTA) syndrome is caused by mutations in
RT FREM1.";
RL J. Med. Genet. 48:375-382(2011).
RN [9]
RP VARIANTS TRIGNO2 GLN-498 AND VAL-1500.
RX PubMed=21931569; DOI=10.1371/journal.pgen.1002278;
RA Vissers L.E.L.M., Cox T.C., Maga A.M., Short K.M., Wiradjaja F.,
RA Janssen I.M., Jehee F., Bertola D., Liu J., Yagnik G., Sekiguchi K.,
RA Kiyozumi D., van Bokhoven H., Marcelis C., Cunningham M.L., Anderson P.J.,
RA Boyadjiev S.A., Passos-Bueno M.R., Veltman J.A., Smyth I., Buckley M.F.,
RA Roscioli T.;
RT "Heterozygous mutations of FREM1 are associated with an increased risk of
RT isolated metopic craniosynostosis in humans and mice.";
RL PLoS Genet. 7:E1002278-E1002278(2011).
RN [10]
RP VARIANT MOTA GLY-102.
RX PubMed=28111185; DOI=10.1016/j.ejmg.2017.01.005;
RA Chacon-Camacho O.F., Zenker M., Schanze D., Ledesma-Gil J., Zenteno J.C.;
RT "Novel FREM1 mutations in a patient with MOTA syndrome: Clinical findings,
RT mutation update and review of FREM1-related disorders literature.";
RL Eur. J. Med. Genet. 60:190-194(2017).
CC -!- FUNCTION: Extracellular matrix protein that plays a role in epidermal
CC differentiation and is required for epidermal adhesion during embryonic
CC development. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FREM2. {ECO:0000269|PubMed:29688405}.
CC -!- INTERACTION:
CC Q5H8C1; Q5SZK8: FREM2; NbExp=2; IntAct=EBI-21460642, EBI-20737564;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250|UniProtKB:Q684R7}.
CC Note=Localizes at the basement membrane zone of embryonic epidermis and
CC hair follicles. {ECO:0000250|UniProtKB:Q684R7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5H8C1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5H8C1-2; Sequence=VSP_047283, VSP_047284;
CC Name=3;
CC IsoId=Q5H8C1-3; Sequence=VSP_015025;
CC Name=4;
CC IsoId=Q5H8C1-4; Sequence=VSP_015026, VSP_015029, VSP_015030,
CC VSP_015031;
CC -!- DOMAIN: The Calx-beta domain binds calcium with high affinity and
CC undergo a major conformational shift upon binding. {ECO:0000250}.
CC -!- DISEASE: Bifid nose, with or without anorectal and renal anomalies
CC (BNAR) [MIM:608980]: A disease characterized by the presence of a bifid
CC nose usually associated with renal agenesis and anorectal
CC malformations. A bifid nose is a congenital deformity due to failure of
CC the paired nasal processes to fuse to a single midline organ during
CC early gestation. {ECO:0000269|PubMed:19732862}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Manitoba oculotrichoanal syndrome (MOTA) [MIM:248450]: A rare
CC condition defined by eyelid colobomas, cryptophthalmos, and
CC anophthalmia/microphthalmia, an aberrant hairline, a bifid or broad
CC nasal tip, and gastrointestinal anomalies such as omphalocele and anal
CC stenosis. {ECO:0000269|PubMed:21507892, ECO:0000269|PubMed:28111185}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Trigonocephaly 2 (TRIGNO2) [MIM:614485]: A keel-shaped
CC deformation of the forehead, caused by premature fusion of the metopic
CC sutures. It results in a triangular shape of the head.
CC {ECO:0000269|PubMed:21931569}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Was termed QBRICK because it contains 12 repeats: 'Q'
CC stands for queen and is taken from the queen being the 12th in a suit
CC of playing card, and 'BRICK' stands for the repeating unit.
CC -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31064.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mendelian genes FRAS1 related extracellular matrix 1
CC (FREM1); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/FREM1";
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DR EMBL; AB160987; BAD89015.1; -; mRNA.
DR EMBL; AK058190; BAB71709.1; -; mRNA.
DR EMBL; BX641104; CAE46048.1; -; mRNA.
DR EMBL; AL354672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031064; AAH31064.2; ALT_INIT; mRNA.
DR CCDS; CCDS47952.1; -. [Q5H8C1-1]
DR CCDS; CCDS55293.1; -. [Q5H8C1-2]
DR RefSeq; NP_001171175.1; NM_001177704.1. [Q5H8C1-2]
DR RefSeq; NP_659403.4; NM_144966.5. [Q5H8C1-1]
DR RefSeq; XP_005251439.1; XM_005251382.3.
DR RefSeq; XP_005251441.1; XM_005251384.4. [Q5H8C1-2]
DR RefSeq; XP_006716792.1; XM_006716729.3. [Q5H8C1-2]
DR AlphaFoldDB; Q5H8C1; -.
DR BioGRID; 127670; 3.
DR CORUM; Q5H8C1; -.
DR IntAct; Q5H8C1; 1.
DR STRING; 9606.ENSP00000412940; -.
DR GlyGen; Q5H8C1; 5 sites.
DR iPTMnet; Q5H8C1; -.
DR PhosphoSitePlus; Q5H8C1; -.
DR BioMuta; FREM1; -.
DR DMDM; 215274141; -.
DR EPD; Q5H8C1; -.
DR jPOST; Q5H8C1; -.
DR MassIVE; Q5H8C1; -.
DR MaxQB; Q5H8C1; -.
DR PaxDb; Q5H8C1; -.
DR PeptideAtlas; Q5H8C1; -.
DR PRIDE; Q5H8C1; -.
DR ProteomicsDB; 62849; -. [Q5H8C1-1]
DR ProteomicsDB; 62850; -. [Q5H8C1-2]
DR ProteomicsDB; 62851; -. [Q5H8C1-3]
DR ProteomicsDB; 62852; -. [Q5H8C1-4]
DR ProteomicsDB; 7166; -.
DR Antibodypedia; 42751; 97 antibodies from 23 providers.
DR DNASU; 158326; -.
DR Ensembl; ENST00000380880.4; ENSP00000370262.3; ENSG00000164946.20. [Q5H8C1-1]
DR Ensembl; ENST00000380894.5; ENSP00000370278.1; ENSG00000164946.20. [Q5H8C1-2]
DR Ensembl; ENST00000427623.5; ENSP00000412597.1; ENSG00000164946.20. [Q5H8C1-4]
DR GeneID; 158326; -.
DR KEGG; hsa:158326; -.
DR MANE-Select; ENST00000380880.4; ENSP00000370262.3; NM_001379081.2; NP_001366010.1.
DR UCSC; uc003zll.4; human. [Q5H8C1-1]
DR CTD; 158326; -.
DR DisGeNET; 158326; -.
DR GeneCards; FREM1; -.
DR GeneReviews; FREM1; -.
DR HGNC; HGNC:23399; FREM1.
DR HPA; ENSG00000164946; Tissue enhanced (endometrium, epididymis).
DR MalaCards; FREM1; -.
DR MIM; 248450; phenotype.
DR MIM; 608944; gene.
DR MIM; 608980; phenotype.
DR MIM; 614485; phenotype.
DR neXtProt; NX_Q5H8C1; -.
DR OpenTargets; ENSG00000164946; -.
DR Orphanet; 217266; BNAR syndrome.
DR Orphanet; 3366; Non-syndromic metopic craniosynostosis.
DR Orphanet; 2717; Oculotrichoanal syndrome.
DR Orphanet; 93100; Renal agenesis, unilateral.
DR PharmGKB; PA134892147; -.
DR VEuPathDB; HostDB:ENSG00000164946; -.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000156990; -.
DR HOGENOM; CLU_001041_0_0_1; -.
DR InParanoid; Q5H8C1; -.
DR OMA; MVYVTDG; -.
DR OrthoDB; 13258at2759; -.
DR PhylomeDB; Q5H8C1; -.
DR TreeFam; TF316876; -.
DR PathwayCommons; Q5H8C1; -.
DR SignaLink; Q5H8C1; -.
DR SIGNOR; Q5H8C1; -.
DR BioGRID-ORCS; 158326; 15 hits in 1069 CRISPR screens.
DR ChiTaRS; FREM1; human.
DR GeneWiki; FREM1; -.
DR GenomeRNAi; 158326; -.
DR Pharos; Q5H8C1; Tbio.
DR PRO; PR:Q5H8C1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5H8C1; protein.
DR Bgee; ENSG00000164946; Expressed in smooth muscle tissue and 114 other tissues.
DR ExpressionAtlas; Q5H8C1; baseline and differential.
DR Genevisible; Q5H8C1; HS.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; IMP:UniProtKB.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045658; FRAS1-rel_N.
DR InterPro; IPR032825; FREM1.
DR PANTHER; PTHR45739:SF7; PTHR45739:SF7; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF19309; Frem_N; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF141072; SSF141072; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS51854; CSPG; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Cell adhesion;
KW Craniosynostosis; Developmental protein; Disease variant; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..2179
FT /note="FRAS1-related extracellular matrix protein 1"
FT /id="PRO_0000010122"
FT REPEAT 296..390
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 413..500
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 521..615
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 642..754
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 776..867
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 887..982
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1024..1126
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1147..1254
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1275..1372
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1393..1485
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1506..1596
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1628..1724
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 1731..1830
FT /note="Calx-beta"
FT DOMAIN 2060..2174
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 199..201
FT /note="Cell attachment site"
FT /evidence="ECO:0000250"
FT MOTIF 1907..1909
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2151..2165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..1803
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015025"
FT VAR_SEQ 1..1587
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015026"
FT VAR_SEQ 1..1464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047283"
FT VAR_SEQ 1465..1480
FT /note="VCYVHKSKVTVSSDRF -> MVTQESMLKAALPLFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047284"
FT VAR_SEQ 1588..1619
FT /note="TDCFTFMATDGTNQGFIVNGRVWEEPVLFTIQ -> MLDESLAVRRSKKCKE
FT MIMHWEKKEDIDIVNT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015029"
FT VAR_SEQ 1804..1809
FT /note="MSTKMW -> SSILCL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015030"
FT VAR_SEQ 1810..2179
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015031"
FT VARIANT 102
FT /note="D -> G (in MOTA; unknown pathological significance;
FT dbSNP:rs1338652795)"
FT /evidence="ECO:0000269|PubMed:28111185"
FT /id="VAR_078339"
FT VARIANT 439
FT /note="V -> L (in dbSNP:rs2779500)"
FT /evidence="ECO:0000269|PubMed:15878328"
FT /id="VAR_047317"
FT VARIANT 498
FT /note="R -> Q (in TRIGNO2; dbSNP:rs184394424)"
FT /evidence="ECO:0000269|PubMed:21931569"
FT /id="VAR_067916"
FT VARIANT 499
FT /note="I -> V (in dbSNP:rs1353223)"
FT /id="VAR_047318"
FT VARIANT 649
FT /note="R -> W (in BNAR; dbSNP:rs121912609)"
FT /evidence="ECO:0000269|PubMed:19732862"
FT /id="VAR_063422"
FT VARIANT 803
FT /note="S -> Y (in dbSNP:rs7023244)"
FT /id="VAR_047319"
FT VARIANT 863
FT /note="L -> V (in dbSNP:rs7041710)"
FT /evidence="ECO:0000269|PubMed:15878328"
FT /id="VAR_047320"
FT VARIANT 1202
FT /note="S -> R (in dbSNP:rs16932300)"
FT /id="VAR_047321"
FT VARIANT 1273
FT /note="D -> E (in dbSNP:rs7025814)"
FT /id="VAR_047322"
FT VARIANT 1324
FT /note="L -> R (in MOTA; dbSNP:rs281875281)"
FT /evidence="ECO:0000269|PubMed:21507892"
FT /id="VAR_066412"
FT VARIANT 1440
FT /note="G -> S (in BNAR; dbSNP:rs121912610)"
FT /evidence="ECO:0000269|PubMed:19732862"
FT /id="VAR_063423"
FT VARIANT 1500
FT /note="E -> V (in TRIGNO2; dbSNP:rs281875280)"
FT /evidence="ECO:0000269|PubMed:21931569"
FT /id="VAR_067917"
FT VARIANT 1502
FT /note="V -> M (in dbSNP:rs10961700)"
FT /id="VAR_047323"
FT VARIANT 1576
FT /note="N -> I (in dbSNP:rs2101770)"
FT /id="VAR_047324"
FT VARIANT 2091
FT /note="V -> I (in MOTA; dbSNP:rs281875282)"
FT /evidence="ECO:0000269|PubMed:21507892"
FT /id="VAR_066413"
FT VARIANT 2143
FT /note="Q -> P (in dbSNP:rs10961689)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15878328"
FT /id="VAR_047325"
FT VARIANT 2174
FT /note="V -> G (in dbSNP:rs17856912)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047326"
FT CONFLICT 1735
FT /note="I -> N (in Ref. 5; AAH31064)"
FT /evidence="ECO:0000305"
FT CONFLICT 1861
FT /note="S -> A (in Ref. 3; CAE46048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2179 AA; 244154 MW; 9C1C464DF95D2194 CRC64;
MNSLSWGAAN AVLLLLLLAW ASPTFISINR GVRVMKGHSA FLSGDDLKFA IPKEKDACKV
EVVMNEPITQ RVGKLTPQVF DCHFLPNEVK YVHNGCPILD EDTVKLRLYR FTERDTFIET
FILWVYLLEP DCNIIHMSNN VLEVPEFNGL SQAIDKNLLR FDYDRMASLE CTVSLDTART
RLPAHGQMVL GEPRPEEPRG DQPHSFFPES QLRAKLKCPG GSCTPGLKKI GSLKVSCEEF
LLMGLRYQHL DPPSPNIDYI SIQLDLTDTR SKIVYKSESA WLPVYIRAGI PNQIPKAAFM
AVFILEVDQF ILTSLTTSVL DCEEDETPKP LLVFNITKAP LQGYVTHLLD HTRPISSFTW
KDLSDMQIAY QPPNSSHSER RHDEVELEVY DFFFERSAPM TVHISIRTAD TNAPRVSWNT
GLSLLEGQSR AITWEQFQVV DNDDIGAVRL VTVGGLQHGW LTLRGGKGFL FTVADLQAGV
VRYHHDDSDS TKDFVVFRIF DGHHSIRHKF PINVLPKDDS PPFLITNVVI ELEEGQTILI
QGSMLRASDV DASDDYIFFN ITKPPQAGEI MKKPGPGLIG YPVHGFLQRD LFNGIIYYRH
FGGEIFEDSF QFVLWDSHEP PNLSVPQVAT IHITPVDDQL PKEAPGVSRH LVVKETEVAY
ITKKQLHFID SESYDRELVY TITTPPFFSF SHRHLDAGKL FMVDSIPKVV KNPTALELRS
FTQHAVNYMK VAYMPPMQDI GPHCRDVQFT FSVSNQHGGT LHGICFNITI LPVDNQVPEA
FTNPLKVTEG GQSIISTEHI LISDADTKLD NIDLSLRELP LHGRVELNGF PLNSGGTFSW
GDLHTLKVRY QHDGTEVLQD DLLLEVTDGT NSAEFVLHVE VFPVNDEPPV LKADLMPVMN
CSEGGEVVIT SEYIFATDVD SDNLKLMFVI AREPQHGVVR RAGVTVDQFS QRDVISEAVT
YKHTGGEIGL MPCFDTITLV VSDGEAGPFV NGCCYNGPNP SVPLHASFPV YDLNITVYPV
DNQPPSIAIG PVFVVDEGCS TALTVNHLSA TDPDTAADDL EFVLVSPPQF GYLENILPSV
GFEKSNIGIS IDSFQWKDMN AFHINYVQSR HLRIEPTADQ FTVYVTDGKH HSLEIPFSII
INPTNDEAPD FVVQNITVCE GQMKELDSSI ISAVDLDIPQ DALLFSITQK PRHGLLIDRG
FSKDFSENKQ PANPHQKHAP VHSFSMELLK TGMRLTYMHD DSESLADDFT IQLSDGKHKI
LKTISVEVIP VNDEKPMLSK KAEIAMNMGE TRIISSAILS AIDEDSPREK IYYVFERLPQ
NGQLQLKIGR DWVPLSPGMK CTQEEVDLNL LRYTHTGAMD SQNQDSFTFY LWDGNNRSPA
LDCQITIKDM EKGDIVILTK PLVVSKGDRG FLTTTTLLAV DGTDKPEELL YVITSPPRYG
QIEYVHYPGV PITNFSQMDV VGQTVCYVHK SKVTVSSDRF RFIISNGLRT EHGVFEITLE
TVDRALPVVT RNKGLRLAQG AVGLLSPDLL QLTDPDTPAE NLTFLLVQLP QHGQLYLWGT
GLLQHNFTQQ DVDSKNVAYR HSGGDSQTDC FTFMATDGTN QGFIVNGRVW EEPVLFTIQV
DQLDKTAPRI TLLHSPSQVG LLKNGCYGIY ITSRVLKASD PDTEDDQIIF KILQGPKHGH
LENTTTGEFI HEKFSQKDLN SKTILYIINP SLEVNSDTVE FQIMDPTGNS ATPQILELKW
SHIEWSQTEY EVCENVGLLP LEIIRRGYSM DSAFVGIKVN QVSAAVGKDF TVIPSKLIQF
DPGMSTKMWN IAITYDGLEE DDEVFEVILN SPVNAVLGTK TKAAVKILDS KGGQCHPSYS
SNQSKHSTWE KGIWHLLPPG SSSSTTSGSF HLERRPLPSS MQLAVIRGDT LRGFDSTDLS
QRKLRTRGNG KTVRPSSVYR NGTDIIYNYH GIVSLKLEDD SFPTHKRKAK VSIISQPQKT
IKVAELPQAD KVESTTDSHF PRQDQLPSFP KNCTLELKGL FHFEEGIQKL YQCNGIAWKA
WSPQTKDVED KSCPAGWHQH SGYCHILITE QKGTWNAAAQ ACREQYLGNL VTVFSRQHMR
WLWDIGGRKS FWIGLNDQVH AGHWEWIGGE PVAFTNGRRG PSQRSKLGKS CVLVQRQGKW
QTKDCRRAKP HNYVCSRKL
