MATN2_HUMAN
ID MATN2_HUMAN Reviewed; 956 AA.
AC O00339; A8K106; E7EW74; E9PD48; E9PGL2; Q6UWA5; Q7Z5X1; Q8NDE6; Q96FT5;
AC Q9NSZ1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Matrilin-2;
DE Flags: Precursor;
GN Name=MATN2; ORFNames=UNQ193/PRO219;
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] (ISOFORMS 1 AND 2).
RX PubMed=11124542; DOI=10.1159/000056797;
RA Muratoglu S., Krysan K., Balazs M., Sheng H., Zakany R., Modis L., Kiss I.,
RA Deak F.;
RT "Primary structure of human matrilin-2, chromosome location of the MATN2
RT gene and conservation of an AT-AC intron in matrilin genes.";
RL Cytogenet. Cell Genet. 90:323-327(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-187.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLU-356.
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 242-956 (ISOFORM 1), AND VARIANT GLU-356.
RC TISSUE=Brain, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 644-956.
RX PubMed=9083061; DOI=10.1074/jbc.272.14.9268;
RA Deak F., Piecha D., Bachrati C., Paulsson M., Kiss I.;
RT "Primary structure and expression of matrilin-2, the closest relative of
RT cartilage matrix protein within the von Willebrand factor type A-like
RT module superfamily.";
RL J. Biol. Chem. 272:9268-9274(1997).
CC -!- FUNCTION: Involved in matrix assembly. {ECO:0000250}.
CC -!- INTERACTION:
CC O00339; O15265: ATXN7; NbExp=2; IntAct=EBI-949020, EBI-708350;
CC O00339; O00555: CACNA1A; NbExp=2; IntAct=EBI-949020, EBI-766279;
CC O00339; O68704: yopK; Xeno; NbExp=2; IntAct=EBI-949020, EBI-20592411;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=O00339-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O00339-2; Sequence=VSP_001399;
CC Name=3;
CC IsoId=O00339-3; Sequence=VSP_013284;
CC Name=4;
CC IsoId=O00339-4; Sequence=VSP_014540;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD38787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U69263; AAC51260.2; -; mRNA.
DR EMBL; AY358895; AAQ89254.1; -; mRNA.
DR EMBL; AL137638; CAB70853.2; -; mRNA.
DR EMBL; AK289721; BAF82410.1; -; mRNA.
DR EMBL; AL833931; CAD38787.1; ALT_INIT; mRNA.
DR EMBL; AP002906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010444; AAH10444.1; -; mRNA.
DR EMBL; BC016394; AAH16394.1; -; mRNA.
DR CCDS; CCDS55264.1; -. [O00339-1]
DR CCDS; CCDS55265.1; -. [O00339-2]
DR CCDS; CCDS83309.1; -. [O00339-3]
DR RefSeq; NP_001304677.1; NM_001317748.1. [O00339-3]
DR RefSeq; NP_002371.3; NM_002380.4. [O00339-1]
DR RefSeq; NP_085072.2; NM_030583.3. [O00339-2]
DR AlphaFoldDB; O00339; -.
DR BioGRID; 110317; 104.
DR ComplexPortal; CPX-4464; Matrilin-2 complex.
DR DIP; DIP-47267N; -.
DR IntAct; O00339; 9.
DR MINT; O00339; -.
DR STRING; 9606.ENSP00000254898; -.
DR GlyGen; O00339; 4 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O00339; -.
DR PhosphoSitePlus; O00339; -.
DR BioMuta; MATN2; -.
DR jPOST; O00339; -.
DR MassIVE; O00339; -.
DR MaxQB; O00339; -.
DR PaxDb; O00339; -.
DR PeptideAtlas; O00339; -.
DR PRIDE; O00339; -.
DR ProteomicsDB; 47856; -. [O00339-1]
DR ProteomicsDB; 47857; -. [O00339-2]
DR ProteomicsDB; 47858; -. [O00339-3]
DR ProteomicsDB; 47859; -. [O00339-4]
DR Antibodypedia; 26033; 186 antibodies from 33 providers.
DR DNASU; 4147; -.
DR Ensembl; ENST00000254898.7; ENSP00000254898.6; ENSG00000132561.14. [O00339-1]
DR Ensembl; ENST00000520016.5; ENSP00000430487.1; ENSG00000132561.14. [O00339-1]
DR Ensembl; ENST00000521689.5; ENSP00000429977.1; ENSG00000132561.14. [O00339-2]
DR Ensembl; ENST00000522025.6; ENSP00000429010.1; ENSG00000132561.14. [O00339-4]
DR Ensembl; ENST00000524308.5; ENSP00000430221.1; ENSG00000132561.14. [O00339-3]
DR GeneID; 4147; -.
DR KEGG; hsa:4147; -.
DR MANE-Select; ENST00000254898.7; ENSP00000254898.6; NM_002380.5; NP_002371.3.
DR UCSC; uc003yic.4; human. [O00339-1]
DR CTD; 4147; -.
DR DisGeNET; 4147; -.
DR GeneCards; MATN2; -.
DR HGNC; HGNC:6908; MATN2.
DR HPA; ENSG00000132561; Low tissue specificity.
DR MIM; 602108; gene.
DR neXtProt; NX_O00339; -.
DR OpenTargets; ENSG00000132561; -.
DR PharmGKB; PA30651; -.
DR VEuPathDB; HostDB:ENSG00000132561; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000158008; -.
DR HOGENOM; CLU_008905_0_0_1; -.
DR InParanoid; O00339; -.
DR OMA; CATEDHA; -.
DR TreeFam; TF330078; -.
DR PathwayCommons; O00339; -.
DR SignaLink; O00339; -.
DR BioGRID-ORCS; 4147; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; MATN2; human.
DR GeneWiki; MATN2; -.
DR GenomeRNAi; 4147; -.
DR Pharos; O00339; Tbio.
DR PRO; PR:O00339; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O00339; protein.
DR Bgee; ENSG00000132561; Expressed in tibia and 201 other tissues.
DR ExpressionAtlas; O00339; baseline and differential.
DR Genevisible; O00339; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; IC:ComplexPortal.
DR Gene3D; 1.20.5.30; -; 1.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR030747; Matrilin-2.
DR InterPro; IPR036337; Matrilin_cc_sf.
DR InterPro; IPR019466; Matrilin_coiled-coil_trimer.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020:SF35; PTHR24020:SF35; 4.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF10393; Matrilin_ccoil; 1.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 10.
DR SMART; SM01279; Matrilin_ccoil; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF57184; SSF57184; 3.
DR SUPFAM; SSF58002; SSF58002; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 9.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50234; VWFA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disulfide bond; EGF-like domain;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..956
FT /note="Matrilin-2"
FT /id="PRO_0000007655"
FT DOMAIN 57..232
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 238..278
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 279..319
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 320..360
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 361..401
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 402..442
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 443..483
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 484..524
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 525..565
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 566..606
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 607..647
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 655..830
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 840..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 917..955
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 242..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 249..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 264..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 283..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 290..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 305..318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 324..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 331..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 346..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 365..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 372..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 387..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 406..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 428..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 447..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 454..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 469..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 488..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 495..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 510..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 529..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 536..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 551..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 570..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 577..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 592..605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 611..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 618..631
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 633..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..284
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014540"
FT VAR_SEQ 361..401
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013284"
FT VAR_SEQ 861..879
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11124542,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_001399"
FT VARIANT 14
FT /note="G -> A (in dbSNP:rs35804177)"
FT /id="VAR_055753"
FT VARIANT 187
FT /note="T -> M (in dbSNP:rs2290472)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_055754"
FT VARIANT 356
FT /note="K -> E (in dbSNP:rs1869609)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_021568"
FT VARIANT 599
FT /note="A -> T (in dbSNP:rs35120814)"
FT /id="VAR_055755"
FT VARIANT 855
FT /note="T -> M (in dbSNP:rs2255317)"
FT /id="VAR_055756"
FT VARIANT 932
FT /note="V -> I (in dbSNP:rs17831160)"
FT /id="VAR_055757"
FT CONFLICT 58
FT /note="L -> P (in Ref. 3; BAF82410)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="E -> V (in Ref. 1; AAC51260)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="R -> G (in Ref. 7; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="L -> F (in Ref. 1; AAC51260)"
FT /evidence="ECO:0000305"
FT CONFLICT 890
FT /note="N -> D (in Ref. 3; BAF82410)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="L -> F (in Ref. 7; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106837 MW; D0868FBF62744EF2 CRC64;
MEKMLAGCFL LILGQIVLLP AEARERSRGR SISRGRHART HPQTALLESS CENKRADLVF
IIDSSRSVNT HDYAKVKEFI VDILQFLDIG PDVTRVGLLQ YGSTVKNEFS LKTFKRKSEV
ERAVKRMRHL STGTMTGLAI QYALNIAFSE AEGARPLREN VPRVIMIVTD GRPQDSVAEV
AAKARDTGIL IFAIGVGQVD FNTLKSIGSE PHEDHVFLVA NFSQIETLTS VFQKKLCTAH
MCSTLEHNCA HFCINIPGSY VCRCKQGYIL NSDQTTCRIQ DLCAMEDHNC EQLCVNVPGS
FVCQCYSGYA LAEDGKRCVA VDYCASENHG CEHECVNADG SYLCQCHEGF ALNPDKKTCT
KIDYCASSNH GCQHECVNTD DSYSCHCLKG FTLNPDKKTC RRINYCALNK PGCEHECVNM
EESYYCRCHR GYTLDPNGKT CSRVDHCAQQ DHGCEQLCLN TEDSFVCQCS EGFLINEDLK
TCSRVDYCLL SDHGCEYSCV NMDRSFACQC PEGHVLRSDG KTCAKLDSCA LGDHGCEHSC
VSSEDSFVCQ CFEGYILRED GKTCRRKDVC QAIDHGCEHI CVNSDDSYTC ECLEGFRLAE
DGKRCRRKDV CKSTHHGCEH ICVNNGNSYI CKCSEGFVLA EDGRRCKKCT EGPIDLVFVI
DGSKSLGEEN FEVVKQFVTG IIDSLTISPK AARVGLLQYS TQVHTEFTLR NFNSAKDMKK
AVAHMKYMGK GSMTGLALKH MFERSFTQGE GARPLSTRVP RAAIVFTDGR AQDDVSEWAS
KAKANGITMY AVGVGKAIEE ELQEIASEPT NKHLFYAEDF STMDEISEKL KKGICEALED
SDGRQDSPAG ELPKTVQQPT ESEPVTINIQ DLLSCSNFAV QHRYLFEEDN LLRSTQKLSH
STKPSGSPLE EKHDQCKCEN LIMFQNLANE EVRKLTQRLE EMTQRMEALE NRLRYR
