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   24-JAN-2024, entry version 170.
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.
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   GlyCosmos; Q5H8C1; 5 sites, No reported glycans.
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; 9606-ENSP00000412940; -.
DR   PeptideAtlas; 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; 116 antibodies from 24 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   AGR; HGNC:23399; -.
DR   CTD; 158326; -.
DR   DisGeNET; 158326; -.
DR   GeneCards; FREM1; -.
DR   GeneReviews; FREM1; -.
DR   HGNC; HGNC:23399; FREM1.
DR   HPA; ENSG00000164946; Tissue enhanced (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; MAMFTLE; -.
DR   OrthoDB; 5470912at2759; -.
DR   PhylomeDB; Q5H8C1; -.
DR   TreeFam; TF316876; -.
DR   PathwayCommons; Q5H8C1; -.
DR   SignaLink; Q5H8C1; -.
DR   SIGNOR; Q5H8C1; -.
DR   BioGRID-ORCS; 158326; 15 hits in 1147 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 116 other cell types or tissues.
DR   ExpressionAtlas; Q5H8C1; baseline and differential.
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:0016020; C: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   CDD; cd00037; CLECT; 1.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR45739:SF7; FRAS1-RELATED EXTRACELLULAR MATRIX PROTEIN 1; 1.
DR   PANTHER; PTHR45739; MATRIX PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF16184; Cadherin_3; 12.
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; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF141072; CalX-like; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS51854; CSPG; 12.
DR   Genevisible; Q5H8C1; HS.
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; uncertain 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
//