ID   MXRA8_HUMAN             Reviewed;         442 AA.
AC   Q9BRK3; B3KTR6; B4DE34; Q5TA39; Q96KC3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   09-APR-2025, entry version 184.
DE   RecName: Full=Matrix remodeling-associated protein 8;
DE   AltName: Full=Limitrin;
DE   Flags: Precursor;
GN   Name=MXRA8;
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).
RC   TISSUE=Brain;
RX   PubMed=14603461; DOI=10.1002/glia.10279;
RA   Yonezawa T., Ohtsuka A., Yoshitaka T., Hirano S., Nomoto H., Yamamoto K.,
RA   Ninomiya Y.;
RT   "Limitrin, a novel immunoglobulin superfamily protein localized to glia
RT   limitans formed by astrocyte endfeet.";
RL   Glia 44:190-204(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANT
RP   ASN-396.
RC   TISSUE=Embryo;
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 GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and Pancreas;
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   [5]
RP   FUNCTION, AND INTERACTION WITH ITGB3.
RX   PubMed=22492581; DOI=10.1002/jbmr.1632;
RA   Jung Y.K., Han S.W., Kim G.W., Jeong J.H., Kim H.J., Choi J.Y.;
RT   "DICAM inhibits osteoclast differentiation through attenuation of the
RT   integrin alphaVbeta3 pathway.";
RL   J. Bone Miner. Res. 27:2024-2034(2012).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=23386276; DOI=10.1093/cvr/cvt019;
RA   Han S.W., Jung Y.K., Lee E.J., Park H.R., Kim G.W., Jeong J.H., Han M.S.,
RA   Choi J.Y.;
RT   "DICAM inhibits angiogenesis via suppression of AKT and p38 MAP kinase
RT   signalling.";
RL   Cardiovasc. Res. 98:73-82(2013).
RN   [7]
RP   PHOSPHORYLATION AT SER-228.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [8]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CHIKUNGUNYA VIRUS
RP   SPIKE GLYCOPROTEIN E2 (MICROBIAL INFECTION).
RX   PubMed=29769725; DOI=10.1038/s41586-018-0121-3;
RA   Zhang R., Kim A.S., Fox J.M., Nair S., Basore K., Klimstra W.B.,
RA   Rimkunas R., Fong R.H., Lin H., Poddar S., Crowe J.E. Jr., Doranz B.J.,
RA   Fremont D.H., Diamond M.S.;
RT   "Mxra8 is a receptor for multiple arthritogenic alphaviruses.";
RL   Nature 557:570-574(2018).
CC   -!- FUNCTION: Transmembrane protein which can modulate activity of various
CC       signaling pathways, probably via binding to integrin ITGAV:ITGB3
CC       (PubMed:22492581, PubMed:23386276). Mediates heterophilic cell-cell
CC       interactions in vitro (By similarity). Inhibits osteoclastogenesis
CC       downstream of TNFSF11/RANKL and CSF1, where it may function by
CC       attenuating signaling via integrin ITGB3 and MAP kinase p38 (By
CC       similarity). Plays a role in cartilage formation where it promotes
CC       proliferation and maturation of growth plate chondrocytes (By
CC       similarity). Stimulates formation of primary cilia in chondrocytes (By
CC       similarity). Enhances expression of genes involved in the hedgehog
CC       signaling pathway in chondrocytes, including the hedgehog signaling
CC       molecule IHH; may also promote signaling via the PTHLH/PTHrP pathway
CC       (By similarity). Plays a role in angiogenesis where it suppresses
CC       migration of endothelial cells and also promotes their apoptosis
CC       (PubMed:23386276). Inhibits VEGF-induced activation of AKT and p38 MAP
CC       kinase in endothelial cells (PubMed:23386276). Also inhibits VTN
CC       (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and activation of
CC       PTK2/FAK (PubMed:23386276). May play a role in the maturation and
CC       maintenance of the blood-brain barrier (By similarity).
CC       {ECO:0000250|UniProtKB:Q9DBV4, ECO:0000269|PubMed:22492581,
CC       ECO:0000269|PubMed:23386276}.
CC   -!- FUNCTION: (Microbial infection) Contributes to arthritogenic alphavirus
CC       pathogenesis and acts as a receptor for these viruses.
CC       {ECO:0000269|PubMed:29769725}.
CC   -!- SUBUNIT: Homodimer in cis (By similarity). Does not appear to form
CC       trans-homodimers (By similarity). Interacts with ITGB3; the interaction
CC       inhibits ITGAV:ITGB3 heterodimer formation (PubMed:22492581).
CC       {ECO:0000250|UniProtKB:Q9DBV4, ECO:0000269|PubMed:22492581}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with chikungunya virus spike
CC       glycoprotein E2. {ECO:0000269|PubMed:29769725}.
CC   -!- INTERACTION:
CC       Q9BRK3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-11721798, EBI-17183751;
CC       Q9BRK3; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-11721798, EBI-12011224;
CC       Q9BRK3; Q86UW9: DTX2; NbExp=3; IntAct=EBI-11721798, EBI-740376;
CC       Q9BRK3; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-11721798, EBI-948296;
CC       Q9BRK3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11721798, EBI-741158;
CC       Q9BRK3; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-11721798, EBI-948354;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23386276};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC       junction {ECO:0000250|UniProtKB:Q9DBV4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9DBV4}. Cell projection, cilium membrane
CC       {ECO:0000250|UniProtKB:Q9DBV4}. Nucleus {ECO:0000269|PubMed:23386276}.
CC       Note=Primarily localizes to the cell membrane (PubMed:23386276).
CC       Detected in the cilium of primary chondrocytes (By similarity). Highly
CC       expressed at areas of cell-cell contact and may localize to tight
CC       junctions (By similarity). Also found in the nucleus where it is
CC       detected in the soluble (as opposed to chromatin-bound) fraction
CC       (PubMed:23386276). {ECO:0000250|UniProtKB:Q9DBV4,
CC       ECO:0000269|PubMed:23386276}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9BRK3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BRK3-2; Sequence=VSP_027448, VSP_027449;
CC       Name=3;
CC         IsoId=Q9BRK3-3; Sequence=VSP_054528;
CC       Name=4;
CC         IsoId=Q9BRK3-4; Sequence=VSP_054529;
CC   -!- TISSUE SPECIFICITY: Detected in endothelial cells in mammary tissue, in
CC       both large vessels (left internal mammary artery) and small capillaries
CC       (vasa vasorum of the adventitia). {ECO:0000269|PubMed:23386276}.
CC   -!- INDUCTION: Up-regulated in vein endothelial cells (HUVECs) in response
CC       to VEGF signaling. {ECO:0000269|PubMed:23386276}.
CC   -!- DOMAIN: The RGD motif is involved in integrin ITGAV:ITGB3 binding.
CC       {ECO:0000250|UniProtKB:Q9DBV4}.
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DR   EMBL; AB052096; BAD05132.1; -; mRNA.
DR   EMBL; AK027269; BAB55010.1; -; mRNA.
DR   EMBL; AK095966; BAG53178.1; -; mRNA.
DR   EMBL; AK293442; BAG56945.1; -; mRNA.
DR   EMBL; AL139287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006213; AAH06213.1; -; mRNA.
DR   EMBL; BC017312; AAH17312.1; -; mRNA.
DR   CCDS; CCDS24.1; -. [Q9BRK3-1]
DR   CCDS; CCDS59950.1; -. [Q9BRK3-4]
DR   CCDS; CCDS59951.1; -. [Q9BRK3-2]
DR   CCDS; CCDS59952.1; -. [Q9BRK3-3]
DR   RefSeq; NP_001269511.1; NM_001282582.2. [Q9BRK3-1]
DR   RefSeq; NP_001269512.1; NM_001282583.2. [Q9BRK3-3]
DR   RefSeq; NP_001269513.1; NM_001282584.2. [Q9BRK3-4]
DR   RefSeq; NP_001269514.1; NM_001282585.1. [Q9BRK3-2]
DR   RefSeq; NP_115724.1; NM_032348.4. [Q9BRK3-1]
DR   PDB; 6JO8; X-ray; 3.50 A; M/N/O=25-292.
DR   PDBsum; 6JO8; -.
DR   AlphaFoldDB; Q9BRK3; -.
DR   SMR; Q9BRK3; -.
DR   BioGRID; 120064; 16.
DR   IntAct; Q9BRK3; 12.
DR   MINT; Q9BRK3; -.
DR   STRING; 9606.ENSP00000399229; -.
DR   GlyCosmos; Q9BRK3; 3 sites, 1 glycan.
DR   GlyGen; Q9BRK3; 4 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (2 sites).
DR   iPTMnet; Q9BRK3; -.
DR   PhosphoSitePlus; Q9BRK3; -.
DR   BioMuta; MXRA8; -.
DR   DMDM; 74761214; -.
DR   jPOST; Q9BRK3; -.
DR   MassIVE; Q9BRK3; -.
DR   PaxDb; 9606-ENSP00000399229; -.
DR   PeptideAtlas; Q9BRK3; -.
DR   ProteomicsDB; 3687; -.
DR   ProteomicsDB; 78776; -. [Q9BRK3-1]
DR   ProteomicsDB; 78777; -. [Q9BRK3-2]
DR   Antibodypedia; 66422; 41 antibodies from 9 providers.
DR   DNASU; 54587; -.
DR   Ensembl; ENST00000309212.11; ENSP00000307887.6; ENSG00000162576.17. [Q9BRK3-1]
DR   Ensembl; ENST00000342753.8; ENSP00000344998.4; ENSG00000162576.17. [Q9BRK3-4]
DR   Ensembl; ENST00000445648.5; ENSP00000399229.2; ENSG00000162576.17. [Q9BRK3-2]
DR   Ensembl; ENST00000477278.3; ENSP00000436135.1; ENSG00000162576.17. [Q9BRK3-3]
DR   GeneID; 54587; -.
DR   KEGG; hsa:54587; -.
DR   MANE-Select; ENST00000309212.11; ENSP00000307887.6; NM_032348.4; NP_115724.1.
DR   UCSC; uc001aew.5; human. [Q9BRK3-1]
DR   AGR; HGNC:7542; -.
DR   CTD; 54587; -.
DR   DisGeNET; 54587; -.
DR   GeneCards; MXRA8; -.
DR   HGNC; HGNC:7542; MXRA8.
DR   HPA; ENSG00000162576; Low tissue specificity.
DR   MalaCards; MXRA8; -.
DR   MIM; 617293; gene.
DR   neXtProt; NX_Q9BRK3; -.
DR   OpenTargets; ENSG00000162576; -.
DR   PharmGKB; PA31343; -.
DR   VEuPathDB; HostDB:ENSG00000162576; -.
DR   eggNOG; ENOG502QRZ7; Eukaryota.
DR   GeneTree; ENSGT00390000001509; -.
DR   HOGENOM; CLU_062248_1_0_1; -.
DR   InParanoid; Q9BRK3; -.
DR   OMA; HIPVACL; -.
DR   OrthoDB; 9832369at2759; -.
DR   PhylomeDB; Q9BRK3; -.
DR   TreeFam; TF332884; -.
DR   PathwayCommons; Q9BRK3; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; Q9BRK3; -.
DR   BioGRID-ORCS; 54587; 14 hits in 1155 CRISPR screens.
DR   ChiTaRS; MXRA8; human.
DR   GenomeRNAi; 54587; -.
DR   Pharos; Q9BRK3; Tdark.
DR   PRO; PR:Q9BRK3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9BRK3; protein.
DR   Bgee; ENSG00000162576; Expressed in stromal cell of endometrium and 181 other cell types or tissues.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; ISS:CAFA.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0060857; P:establishment of glial blood-brain barrier; ISS:CAFA.
DR   FunFam; 2.60.40.10:FF:000806; Matrix remodeling associated 8; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR042472; MXRA8.
DR   PANTHER; PTHR44793; MATRIX REMODELING-ASSOCIATED PROTEIN 8; 1.
DR   PANTHER; PTHR44793:SF1; MATRIX REMODELING-ASSOCIATED PROTEIN 8; 1.
DR   Pfam; PF07686; V-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00406; IGv; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Cytoplasm; Disulfide bond; Glycoprotein;
KW   Host-virus interaction; Immunoglobulin domain; Membrane; Nucleus;
KW   Phosphoprotein; Proteomics identification; Reference proteome; Repeat;
KW   Signal; Tight junction; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..442
FT                   /note="Matrix remodeling-associated protein 8"
FT                   /id="PRO_0000298665"
FT   TOPO_DOM        20..341
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..442
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..157
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          160..288
FT                   /note="Ig-like V-type 2"
FT   REGION          294..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           252..254
FT                   /note="RGD"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBV4"
FT   SITE            325..326
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XI43"
FT   MOD_RES         228
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        186..272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         1..17
FT                   /note="MALPSRILLWKLVLLQS -> MIRCAATG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054528"
FT   VAR_SEQ         25..125
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054529"
FT   VAR_SEQ         407
FT                   /note="L -> LASSPPT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_027448"
FT   VAR_SEQ         435..442
FT                   /note="GFRKENCK -> DPSGLCPLGA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_027449"
FT   VARIANT         396
FT                   /note="D -> N (in dbSNP:rs150058708)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_070893"
FT   CONFLICT        405
FT                   /note="I -> V (in Ref. 2; BAB55010)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          69..77
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          86..95
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            103..107
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          133..140
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          151..160
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          170..180
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          220..228
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            237..241
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          242..245
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            247..250
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          257..261
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          268..275
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   TURN            277..280
FT                   /evidence="ECO:0007829|PDB:6JO8"
FT   STRAND          284..291
FT                   /evidence="ECO:0007829|PDB:6JO8"
SQ   SEQUENCE   442 AA;  49132 MW;  B08F89D726222CA1 CRC64;
     MALPSRILLW KLVLLQSSAV LLHSGSSVPA AAGSSVVSES AVSWEAGARA VLRCQSPRMV
     WTQDRLHDRQ RVLHWDLRGP GGGPARRLLD LYSAGEQRVY EARDRGRLEL SASAFDDGNF
     SLLIRAVEET DAGLYTCNLH HHYCHLYESL AVRLEVTDGP PATPAYWDGE KEVLAVARGA
     PALLTCVNRG HVWTDRHVEE AQQVVHWDRQ PPGVPHDRAD RLLDLYASGE RRAYGPLFLR
     DRVAVGADAF ERGDFSLRIE PLEVADEGTY SCHLHHHYCG LHERRVFHLT VAEPHAEPPP
     RGSPGNGSSH SGAPGPDPTL ARGHNVINVI VPESRAHFFQ QLGYVLATLL LFILLLVTVL
     LAARRRRGGY EYSDQKSGKS KGKDVNLAEF AVAAGDQMLY RSEDIQLDYK NNILKERAEL
     AHSPLPAKYI DLDKGFRKEN CK
//