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 27-MAR-2024, entry version 213. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 106. DR ComplexPortal; CPX-4464; Matrilin-2 complex. DR DIP; DIP-47267N; -. DR IntAct; O00339; 9. DR MINT; O00339; -. DR STRING; 9606.ENSP00000254898; -. DR GlyCosmos; O00339; 4 sites, 1 glycan. DR GlyGen; O00339; 8 sites, 3 O-linked glycans (7 sites). DR iPTMnet; O00339; -. DR PhosphoSitePlus; O00339; -. DR BioMuta; MATN2; -. DR jPOST; O00339; -. DR MassIVE; O00339; -. DR MaxQB; O00339; -. DR PaxDb; 9606-ENSP00000254898; -. DR PeptideAtlas; O00339; -. DR ProteomicsDB; 47856; -. [O00339-1] DR ProteomicsDB; 47857; -. [O00339-2] DR ProteomicsDB; 47858; -. [O00339-3] DR ProteomicsDB; 47859; -. [O00339-4] DR Antibodypedia; 26033; 216 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 AGR; HGNC:6908; -. 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 OrthoDB; 1453590at2759; -. DR TreeFam; TF330078; -. DR PathwayCommons; O00339; -. DR SignaLink; O00339; -. DR BioGRID-ORCS; 4147; 10 hits in 1149 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 203 other cell types or tissues. DR ExpressionAtlas; O00339; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. 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:0120216; C:matrilin complex; ISO:ComplexPortal. 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:0007411; P:axon guidance; IEA:Ensembl. DR GO; GO:0031104; P:dendrite regeneration; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; NAS:ComplexPortal. DR GO; GO:0008347; P:glial cell migration; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR CDD; cd00054; EGF_CA; 2. DR CDD; cd01475; vWA_Matrilin; 2. DR Gene3D; 1.20.5.30; -; 1. DR Gene3D; 2.10.25.10; Laminin; 10. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; 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; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24020:SF35; MATRILIN-2; 1. DR Pfam; PF12662; cEGF; 1. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF14670; FXa_inhibition; 8. DR Pfam; PF10393; Matrilin_ccoil; 1. DR Pfam; PF00092; VWA; 2. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00181; EGF; 10. DR SMART; SM00179; EGF_CA; 10. DR SMART; SM01279; Matrilin_ccoil; 1. DR SMART; SM00327; VWA; 2. DR SUPFAM; SSF58002; Chicken cartilage matrix protein; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 3. DR SUPFAM; SSF53300; vWA-like; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 9. DR PROSITE; PS01186; EGF_2; 9. DR PROSITE; PS50026; EGF_3; 4. DR PROSITE; PS50234; VWFA; 2. DR Genevisible; O00339; HS. 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 //