ID   FRAS1_MOUSE             Reviewed;        4010 AA.
AC   Q80T14; E9QPG9; Q80TC7; Q811H8; Q8BPZ4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Extracellular matrix organizing protein FRAS1 {ECO:0000303|PubMed:32333816};
DE   Flags: Precursor;
GN   Name=Fras1 {ECO:0000312|MGI:MGI:2385368}; Synonyms=Kiaa1500;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND DISEASE.
RC   STRAIN=NMRI; TISSUE=Brain;
RX   PubMed=12766770; DOI=10.1038/ng1168;
RA   Vrontou S., Petrou P., Meyer B.I., Vassilis K., Galanopoulos K., Imai K.,
RA   Yanagi M., Chowdhury K., Scambler P.J., Chalepakis G.;
RT   "Fras1 deficiency results in cryptophthalmos, renal agenesis and blebbed
RT   phenotype in mice.";
RL   Nat. Genet. 34:209-214(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2283-4010.
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2646-4010.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3228-4010.
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISEASE.
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND DISEASE.
RX   PubMed=32333816; DOI=10.1111/ejn.14759;
RA   Kalpachidou T., Makrygiannis A.K., Pavlakis E., Stylianopoulou F.,
RA   Chalepakis G., Stamatakis A.;
RT   "Behavioural effects of extracellular matrix protein Fras1 depletion in the
RT   mouse.";
RL   Eur. J. Neurosci. 53:3905-3919(2021).
CC   -!- FUNCTION: Involved in extracellular matrix organization
CC       (PubMed:32333816). Required for the regulation of epidermal-basement
CC       membrane adhesion responsible for proper organogenesis during embryonic
CC       development (PubMed:12766769). Involved in brain organization and
CC       function (PubMed:32333816). {ECO:0000269|PubMed:12766769,
CC       ECO:0000269|PubMed:32333816}.
CC   -!- INTERACTION:
CC       Q80T14; Q6NVD0: Frem2; NbExp=2; IntAct=EBI-15594303, EBI-15594269;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12766769,
CC       ECO:0000269|PubMed:32333816}; Single-pass type I membrane protein
CC       {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:12766769,
CC       ECO:0000269|PubMed:32333816}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the apical ectodermal ridge of
CC       the limb buds from 10.5-12.5 dpc and expression was also detected in
CC       the interdigital spaces at 14.5 dpc. Found in cells just underlying the
CC       surface epithelium of the entire embryo and in the linings of the
CC       peritoneal cavity and dorsal aorta. At 12 dpc, detected in the
CC       mesonephric duct and in the lens (PubMed:12766769). Found in a linear
CC       fashion underlying the epidermis and the basal surface of other
CC       epithelia in embryos (PubMed:12766770). Found in meningeal and
CC       choroidal epidermal-basement membranes in embryos and neonates
CC       (PubMed:32333816). {ECO:0000269|PubMed:12766769,
CC       ECO:0000269|PubMed:12766770, ECO:0000269|PubMed:32333816}.
CC   -!- DOMAIN: The Calx-beta domains bind calcium with high affinity and
CC       undergo a major conformational shift upon binding. {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in Fras1 are the cause of blebbed (bl) phenotype,
CC       which is characterized by blister formation, syndactyly, eyelid fusion
CC       and renal agenesis. Subepidermal blisters are predominantly formed in
CC       the head region around the eyes and at the distal part of the limbs. As
CC       development proceeds blisters that are initially transparent gradually
CC       become hemorrhagic and embryos die between 14.5 dpc and 16.5 dpc.
CC       {ECO:0000269|PubMed:12766769, ECO:0000269|PubMed:12766770,
CC       ECO:0000269|PubMed:32333816}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous adult knockout mice display impaired
CC       performance in various types of learning and memory tasks as well as
CC       reduced anxiety. {ECO:0000269|PubMed:32333816}.
CC   -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC34788.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC34788.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ489280; CAD33519.1; -; mRNA.
DR   EMBL; AC101391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK122518; BAC65800.1; -; mRNA.
DR   EMBL; AK051850; BAC34788.1; ALT_SEQ; mRNA.
DR   EMBL; BC044881; AAH44881.1; -; mRNA.
DR   CCDS; CCDS19450.1; -.
DR   RefSeq; NP_780682.3; NM_175473.3.
DR   SMR; Q80T14; -.
DR   BioGRID; 231125; 1.
DR   CORUM; Q80T14; -.
DR   DIP; DIP-61242N; -.
DR   IntAct; Q80T14; 2.
DR   STRING; 10090.ENSMUSP00000043250; -.
DR   GlyConnect; 2307; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q80T14; 16 sites, 1 glycan.
DR   GlyGen; Q80T14; 16 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q80T14; -.
DR   PhosphoSitePlus; Q80T14; -.
DR   SwissPalm; Q80T14; -.
DR   EPD; Q80T14; -.
DR   MaxQB; Q80T14; -.
DR   PaxDb; 10090-ENSMUSP00000043250; -.
DR   PeptideAtlas; Q80T14; -.
DR   ProteomicsDB; 267408; -.
DR   Antibodypedia; 2470; 46 antibodies from 10 providers.
DR   DNASU; 231470; -.
DR   Ensembl; ENSMUST00000036019.5; ENSMUSP00000043250.5; ENSMUSG00000034687.9.
DR   GeneID; 231470; -.
DR   KEGG; mmu:231470; -.
DR   UCSC; uc008yfk.1; mouse.
DR   AGR; MGI:2385368; -.
DR   CTD; 80144; -.
DR   MGI; MGI:2385368; Fras1.
DR   VEuPathDB; HostDB:ENSMUSG00000034687; -.
DR   eggNOG; KOG1025; Eukaryota.
DR   eggNOG; KOG1216; Eukaryota.
DR   eggNOG; KOG1306; Eukaryota.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; KOG3597; Eukaryota.
DR   GeneTree; ENSGT00940000162130; -.
DR   HOGENOM; CLU_000244_0_0_1; -.
DR   InParanoid; Q80T14; -.
DR   OMA; NSGMRVQ; -.
DR   OrthoDB; 5470912at2759; -.
DR   PhylomeDB; Q80T14; -.
DR   TreeFam; TF316876; -.
DR   BioGRID-ORCS; 231470; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Fras1; mouse.
DR   PRO; PR:Q80T14; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q80T14; Protein.
DR   Bgee; ENSMUSG00000034687; Expressed in fourth ventricle and 212 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IMP:MGI.
DR   GO; GO:0003338; P:metanephros morphogenesis; IMP:MGI.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IMP:MGI.
DR   GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   CDD; cd00064; FU; 12.
DR   Gene3D; 2.60.40.2030; -; 5.
DR   Gene3D; 6.20.200.20; -; 5.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
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   PANTHER; PTHR45739:SF1; EXTRACELLULAR MATRIX ORGANIZING PROTEIN FRAS1; 1.
DR   PANTHER; PTHR45739; MATRIX PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF16184; Cadherin_3; 12.
DR   Pfam; PF03160; Calx-beta; 5.
DR   Pfam; PF00093; VWC; 5.
DR   SMART; SM00237; Calx_beta; 5.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00261; FU; 14.
DR   SMART; SM00214; VWC; 6.
DR   SMART; SM00215; VWC_out; 3.
DR   SUPFAM; SSF141072; CalX-like; 5.
DR   SUPFAM; SSF57603; FnI-like domain; 6.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 5.
DR   PROSITE; PS51854; CSPG; 12.
DR   PROSITE; PS01208; VWFC_1; 6.
DR   PROSITE; PS50184; VWFC_2; 6.
DR   Genevisible; Q80T14; MM.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Glycoprotein; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..4010
FT                   /note="Extracellular matrix organizing protein FRAS1"
FT                   /id="PRO_0000010121"
FT   TOPO_DOM        26..3903
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3904..3924
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3925..4010
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..87
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          92..152
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          156..216
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          218..278
FT                   /note="VWFC 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          282..342
FT                   /note="VWFC 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          358..416
FT                   /note="VWFC 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REPEAT          408..459
FT                   /note="FU 1"
FT   REPEAT          461..504
FT                   /note="FU 2"
FT   REPEAT          506..552
FT                   /note="FU 3"
FT   REPEAT          554..598
FT                   /note="FU 4"
FT   REPEAT          601..646
FT                   /note="FU 5"
FT   REPEAT          648..704
FT                   /note="FU 6"
FT   REPEAT          707..752
FT                   /note="FU 7"
FT   REPEAT          754..799
FT                   /note="FU 8"
FT   REPEAT          802..851
FT                   /note="FU 9"
FT   REPEAT          853..899
FT                   /note="FU 10"
FT   REPEAT          902..947
FT                   /note="FU 11"
FT   REPEAT          951..996
FT                   /note="FU 12"
FT   REPEAT          998..1041
FT                   /note="FU 13"
FT   REPEAT          1045..1088
FT                   /note="FU 14"
FT   REPEAT          1101..1196
FT                   /note="CSPG 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1216..1307
FT                   /note="CSPG 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1328..1440
FT                   /note="CSPG 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1465..1561
FT                   /note="CSPG 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1597..1691
FT                   /note="CSPG 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1712..1812
FT                   /note="CSPG 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1834..1938
FT                   /note="CSPG 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1959..2059
FT                   /note="CSPG 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          2080..2179
FT                   /note="CSPG 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          2201..2293
FT                   /note="CSPG 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          2313..2406
FT                   /note="CSPG 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          2441..2538
FT                   /note="CSPG 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   DOMAIN          2545..2648
FT                   /note="Calx-beta 1"
FT   DOMAIN          2661..2772
FT                   /note="Calx-beta 2"
FT   DOMAIN          2786..2892
FT                   /note="Calx-beta 3"
FT   DOMAIN          2907..3009
FT                   /note="Calx-beta 4"
FT   DOMAIN          3027..3131
FT                   /note="Calx-beta 5"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86XX4"
FT   CARBOHYD        727
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1094
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1779
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1950
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1980
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2684
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2910
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2987
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3072
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3678
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3877
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        22
FT                   /note="N -> H (in Ref. 1; CAD33519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1026
FT                   /note="L -> F (in Ref. 1; CAD33519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1063
FT                   /note="R -> Q (in Ref. 1; CAD33519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1466
FT                   /note="P -> H (in Ref. 1; CAD33519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2020
FT                   /note="N -> H (in Ref. 1; CAD33519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2208
FT                   /note="R -> K (in Ref. 1; CAD33519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2310
FT                   /note="V -> L (in Ref. 1; CAD33519 and 3; BAC65800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2314
FT                   /note="R -> Q (in Ref. 1; CAD33519 and 3; BAC65800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2623
FT                   /note="G -> S (in Ref. 1; CAD33519 and 3; BAC65800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2646
FT                   /note="G -> W (in Ref. 4; BAC34788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2664
FT                   /note="V -> I (in Ref. 1; CAD33519 and 3; BAC65800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3135
FT                   /note="L -> P (in Ref. 1; CAD33519 and 3; BAC65800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3172
FT                   /note="D -> G (in Ref. 4; BAC34788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3383
FT                   /note="Q -> R (in Ref. 1; CAD33519, 3; BAC65800 and 5;
FT                   AAH44881)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3395
FT                   /note="N -> D (in Ref. 1; CAD33519, 3; BAC65800 and 5;
FT                   AAH44881)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4010 AA;  442369 MW;  7C1DDED1C8ACEC04 CRC64;
     MGVLKAWLGV ALALAEFAVL PNCEGACLYQ GSFLADATIW KPDSCQNCRC HGDIVICKPV
     VCKNPRCAFE KGEVLWIAPN QCCPQCAPRT PGSCHHEGKI HEHGTEWASA PCTVCSCTHG
     EVRCSHQQCT PLSCGPQELE FLAEGRCCPI CVGTGKPCSY DGHVFQDGED WQLSRCAKCV
     CRNGLTQCFA AQCQPLFCNQ DEIVVRVPGK CCSQCSARSC STAGQVYEHG EQWKEDACTL
     CMCDQGQVRC HKQVCPPLRC AKGQGRARHH GQCCEECATP DRSCSSGGVL RYQDEMWKGS
     ACEFCMCDQG QVTCQTGECA KVACALGEEL VHLEGKCCPE CISRNGYCIY EQKAETMSSS
     AREIKHVPDG EKWEEGPCKL CECREAQVTC YEPSCPPCPV ATLALVVKGQ CCPDCTPVHC
     HPDCLTCSHS PDHCDLCQDP TKLLQNGRCV HSCGLGFYQA GSLCLACQPQ CSTCTNGLEC
     SSCLPPLLMQ QGQCVSTCGD GFYQDHHSCA VCHESCAGCW GPTEKHCMAC RDPLQVLRDS
     SCENTCGNGF YNRQGTCVAC DQSCKSCGPS SPRCLSCAEK TILHDGKCIS ECPHGYYADS
     TGSCKVCHSS CASCSGPTAA HCIACIHPQT LRQGHCLPSC GEGFYPDHGI CEACHASCHT
     CVGPQPSHCT QCKKPEAGLL VEQHSGENVP YGKCVSRCGT HFYLESTGLC EVCHPSCLTC
     EGKSPHNCTG CESTHALLAG CCVSQCPETH FNLEGTCTEC HPSCRQCHGP LESDCVSCHP
     HLTLTSGHCK TSCKEEQFLN LVGYCADCHP LCQHCVANLQ DTGSICLKCQ HARHLLLGDH
     CVPECPPGHY KERGTCKTCH SSCRSCQNGG PFSCSSCDTG LVLTHIGTCS TACFPGHYLD
     DNQVCQPCNR HCRSCDSQGS CTSCRDPSKV LLFGECQYES CTPQYYLDIA TKTCKECDWS
     CNACTGPLRT DCLQCMDGYV LQDGVCVEQC SPQHYRDSGS CKRCDSHCVE CQGPHECTRC
     EEPFLLFQAQ CVQECGKGYF ADHAKHRCIA CPQGCLRCSH KDRCHLCDHS FFLKSGLCMP
     TCVPGFSGHS SNENCTDKMY TPSLHVNGSL TLGIGSMKPL DFSLLNIQHQ DGRVEDLLFH
     VVSTPTNGQL LLSRNGKEVQ LEKAGHFSWK DVNEKKVRFV HSKEKLRKGY FSLKISDQQF
     FSEPQLINIQ AFSTQAPYVL RNEVLHVSKG ERATITTQLL DIRDDDNPQD VVVNVLDPPL
     HGQLLQMPPA PAASIYQFHL DELSRGLLLY AHDGSDSTSD IIVFQANDGH SFQNILFHVK
     NIPKNDRALR LVTNSMVWVP EGGMLKITNR ILKAQAPGVR ADDIIYKITH SRPQFGEVVL
     LMNLPADSPA GPAEEGHHLP DGRMATPIST FTQQDIDDGV VWYRHLGAPT QSDSFRFQVS
     SATSAQEHLE SHMFNIAILP QAPEAPKLSL GTSLHMTARE DGLSVIQPQS LSFVKAESPS
     GKIIYNITVP LHPNQGIIEH RDRPHSPIQY FTQEDINQGQ IMYRPPVAPP HLQEIMAFSF
     AGLPESVKFY FTVSDGQHTS PEMALTIHLL HSDLQPPAFQ VKAPLLEVSP GGRTSLGLQL
     LVRDAQVVPE ELFFQLQKSP QHGMLVKYTA KSSVTMAAGD TFTYDEVERN VLQYVHDGSS
     AWEDSLEISV TDGLTVTTSE VKVEVSPSEN RGPRLAPGSS LSMTVASQHT AIITRSHLAY
     VDDSSSDPEI WIRLSSLPLY GVLFRSSGPD MDELSGDSNF TMEDINKKNI RYSAVFETDG
     HSVTDGFHFS VSDMDGNHVD NQVFTITVTP AENPPHIIAF ADLITVDEGG RAPLSLHHFF
     ATEDQDNLQD DAVIKLSALP KYGCIENTGT GDRFGPGANS ELEASFPIQD VLENYIYYFQ
     SVHESIEPTH DVFSFYVSDG SGRSEIHSIN ITIERKNDEP PRMTLRPLGV RLSSGVAISN
     SSLSLQDLDT PDNELIFVLM KKPDHGHLLR RSTASDPLEN GTVLDQGSSF TYQDVLAGLV
     GYLPGDIYMA VDEFRFSLTD GLHVDTGRME IYIELPSTNI PHLAINRGLQ LSAGSVARIT
     EQHLKATDTD SEAGQVVYIM KEDPGAGRLL MAKADNLEQI SVRGPIRSFT QADVSQGQIE
     YSHGPGEPGG SFAFKFDVVD GEGNKLADQS FSIGVLEDKS PPVVITNRGL VLDENSVEKI
     TTAQLSATDQ DSKPTELIYR ITTQPQLGHL EHVASPGIQI SSFTQADLAS RNVQYVRSSG
     TGKQSDAFSF VLSDGLHEVT QTFPITIHPV DDARPLVQNR GMRVQEGVRK TITEFELKAV
     DVDTEAESIT FTIVQPPRHG TIERTARGQR FHQTSSFTME DIYQNRVSYS HDGSNSLKDR
     FTFTVSDGTN PFFIIEEGGE EIMTAAPQQF HVDILPVDDG TPRIVTNLGL QWLEYMDGKA
     TNLITKKELL TVDPDTEDSQ LIYEVTTGPM HGYLENKLQP GRAAATFTQE HVNLGLIRYV
     LYEEKIQKVM DSFQFLVKDS KPNVVSDNVF HIQWSLISFK YTSYNVSEKA GSVSVTVQRT
     GNLNQYAIVL CRTEQGTASS SSHPGQQDYM EYAGQVQFDE GEGTKSCTVI INDDDVFENI
     ESFTVGLSMP AYALLGEFTQ AKVVINDTED EPTLEFDKKT YRVNESAGFL FAPIKRQGDS
     SSTVSAVCYT VPKSAMGSSL YALESGSDFK SRGRSAESRV IFGPGVTVST CDVMVIDDSE
     YEEEEEFEIA LADASNNARI GRQAVAKVLI SGPNDASTVS LGNTAFTISE DAGTVKIPVI
     RHGTDLSTFT SVWCATRPSD PASATPGVDY VPSSRKVEFG PGITEQYCTL TILDDTQYPV
     IEGLETFVVF LSSAQGAELT KPSQAVIAIN DTFQDVPSMQ FSKDLLLVKE KEGVLHIPII
     RSGDLSYESS VRCYTQGHSA QVMEDFEERR NADSSRITFL KGQKTKNCTV YIHDDSMFEP
     EEQFRVYLGH PLGNHWSGAR IGKNSVATVT ISNDEDAPTI EFEEAAYQVR EPAGPEAIAV
     LSIKVIRRGD QNRTSKIRCS TRDGSAQSGV DYYPKSRVLK FSPGVDHIFF KVEILSNEDR
     EWHESFSLVL GPDDLVEAVL GDVTTATVTI LDQEAAGSLI LPAPPIVVTL ADYDHVEELA
     KEGVKKAPSP GYPLVCVTPC DPRYPRYAVM KERCSEAGIN QTSVQFSWEV AAPTDGNGAR
     SPFETITDNT PFTSVNHKVL DSIYFSRRFH VRCVAKAVDK VGHVGTPLRS NVVTIGTDSA
     ICHTPVVAGT ARGFQAQSFI ATLKYLDVKH KEHPNRIHIS VQIPHQDGML PLISTMPLHN
     LHFLLSESIY RHQHVCSNLV TAQDLRGLAE AGFLNDAGFH STALGPGYDR PFQFDSSVRE
     PKTIQLYRHL NLKSCVWTFD AYYDMTELID VCGGSVTADF QVRDSAQSFL TVHVPLYVSY
     IYVTAPRGWA SLEHHTEMEF SFFYDTVLWR TGIQTDSVLS ARLQIIRIYI REDGRLVIEF
     KTHAKFRGQF VIEHHTLPDV KSFILTPDHL GGIQFDLQLL WSAQTFDSPH QLWRATSSYN
     RKDYSGEYTI YLIPCTVQPT QPWVDPGEKA LACTAHAPER FLIPIAFQQT NRPVPVVYSL
     NTEFQLCNNE KVFLMDPNTS DMSLAEMDYK GAFSKGQILY GRVLWNPEQN LHSAYKLQLE
     KVYLCTGKDG YVPFFDPTGT IYNEGPQYGC IQPNKHLKHR FLLLDRSQPE VTDKYFHDVP
     FEAHFASELP DFQVVSSMPG VDGFTLKVDA LYKVEAGHQW YLQVIYIIGP DSTSRPRVQR
     SLTVSLRRHQ RDLVDPSGWL SLDDSLIYDN EGDQVKNGTN MKSLNLEMQE PVIAASLSQT
     GASIGSALAA IMLLLLLFLV ACFVTRKCQK QKKKQPPEDT LEEYPLNTKV DVAKRNADKV
     EKNANRQYCT VRNVNILSDN EGYYTFKGAK VKKLNLEVRV HNNLQDGTEV
//