MTMRE_HUMAN
ID MTMRE_HUMAN Reviewed; 650 AA.
AC Q8NCE2; Q0JTH5; Q0JU83; Q6PIZ4; Q6QE21; Q86VK9; Q8IYK1; Q8TCM7; Q9H6C0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Myotubularin-related protein 14;
DE EC=3.1.3.-;
DE AltName: Full=HCV NS5A-transactivated protein 4 splice variant A-binding protein 1;
DE Short=NS5ATP4ABP1;
DE AltName: Full=hJumpy;
GN Name=MTMR14; Synonyms=C3orf29;
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 2).
RA Chen L.D., Cheng J., Wang Q., Hong Y., Zhang L.F., Han L., Yuan J.;
RT "Screening and cloning of interaction protein 1 of HCV NS5A-transactivated
RT protein 4 splice variant A.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Kidney epithelium, and Teratocarcinoma;
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=Brain;
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 MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Duodenal adenocarcinoma, Leukocyte, Retinal pigment epithelium, and
RC Rhabdomyosarcoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 403-557 (ISOFORM 1).
RC TISSUE=Melanoma;
RA Sales M.M., Ferrasi A.C., Pereira A.A., Pardini M.I.M.C., Sogayar M.C.,
RA Camargo A.A.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INVOLVEMENT IN CNM1 AS MODIFIER OF PHENOTYPE, VARIANTS CNM1
RP GLN-336 AND CYS-462, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-330.
RX PubMed=17008356; DOI=10.1093/hmg/ddl250;
RA Tosch V., Rohde H.M., Tronchere H., Zanoteli E., Monroy N., Kretz C.,
RA Dondaine N., Payrastre B., Mandel J.-L., Laporte J.;
RT "A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating
RT variant in centronuclear myopathy.";
RL Hum. Mol. Genet. 15:3098-3106(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-530 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-638, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Lipid phosphatase which efficiently dephosphorylates
CC phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive
CC toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
CC {ECO:0000269|PubMed:17008356}.
CC -!- INTERACTION:
CC Q8NCE2; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-5658424, EBI-11952721;
CC Q8NCE2; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-5658424, EBI-10175039;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17008356}.
CC Note=Found in reticular structures and plasma membrane ruffles.
CC Concentrated near the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NCE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCE2-2; Sequence=VSP_021586;
CC Name=3;
CC IsoId=Q8NCE2-3; Sequence=VSP_021585, VSP_021586;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues, including heart,
CC skeletal muscle, placenta, liver, lung, kidney and pancreas.
CC {ECO:0000269|PubMed:17008356}.
CC -!- DISEASE: Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital
CC muscle disorder characterized by progressive muscular weakness and
CC wasting involving mainly limb girdle, trunk, and neck muscles. It may
CC also affect distal muscles. Weakness may be present during childhood or
CC adolescence or may not become evident until the third decade of life.
CC Ptosis is a frequent clinical feature. The most prominent
CC histopathologic features include high frequency of centrally located
CC nuclei in muscle fibers not secondary to regeneration, radial
CC arrangement of sarcoplasmic strands around the central nuclei, and
CC predominance and hypotrophy of type 1 fibers.
CC {ECO:0000269|PubMed:17008356}. Note=The gene represented in this entry
CC may act as a disease modifier. MTMR14 mutations affecting enzymatic
CC function have been found in sporadic cases of centronuclear myopathy,
CC one of them carrying a disease-associated mutation in DNM2
CC (PubMed:17008356). This raises the possibility of MTMR14 being a
CC modifier of the phenotype in some cases of centronuclear myopathy
CC (PubMed:17008356). {ECO:0000269|PubMed:17008356}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15340.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ630520; ABG02221.1; -; mRNA.
DR EMBL; AK026058; BAB15340.1; ALT_INIT; mRNA.
DR EMBL; AK074792; BAC11211.1; -; mRNA.
DR EMBL; AL713695; CAD28494.1; -; mRNA.
DR EMBL; AM393309; CAL38187.1; -; mRNA.
DR EMBL; AM393050; CAL37928.1; -; mRNA.
DR EMBL; BC001674; AAH01674.2; -; mRNA.
DR EMBL; BC025952; AAH25952.2; -; mRNA.
DR EMBL; BC035690; AAH35690.1; -; mRNA.
DR EMBL; BC050626; AAH50626.1; -; mRNA.
DR EMBL; AY545552; AAS50151.1; -; mRNA.
DR CCDS; CCDS43043.1; -. [Q8NCE2-1]
DR CCDS; CCDS43044.1; -. [Q8NCE2-2]
DR CCDS; CCDS43045.1; -. [Q8NCE2-3]
DR RefSeq; NP_001070993.1; NM_001077525.2. [Q8NCE2-1]
DR RefSeq; NP_001070994.1; NM_001077526.2. [Q8NCE2-2]
DR RefSeq; NP_071930.2; NM_022485.4. [Q8NCE2-3]
DR AlphaFoldDB; Q8NCE2; -.
DR BioGRID; 122168; 107.
DR IntAct; Q8NCE2; 41.
DR MINT; Q8NCE2; -.
DR STRING; 9606.ENSP00000296003; -.
DR DEPOD; MTMR14; -.
DR GlyGen; Q8NCE2; 2 sites.
DR iPTMnet; Q8NCE2; -.
DR PhosphoSitePlus; Q8NCE2; -.
DR BioMuta; MTMR14; -.
DR DMDM; 118568016; -.
DR EPD; Q8NCE2; -.
DR jPOST; Q8NCE2; -.
DR MassIVE; Q8NCE2; -.
DR MaxQB; Q8NCE2; -.
DR PaxDb; Q8NCE2; -.
DR PeptideAtlas; Q8NCE2; -.
DR PRIDE; Q8NCE2; -.
DR ProteomicsDB; 72881; -. [Q8NCE2-1]
DR ProteomicsDB; 72882; -. [Q8NCE2-2]
DR ProteomicsDB; 72883; -. [Q8NCE2-3]
DR Antibodypedia; 25426; 269 antibodies from 26 providers.
DR DNASU; 64419; -.
DR Ensembl; ENST00000296003.9; ENSP00000296003.5; ENSG00000163719.20. [Q8NCE2-1]
DR Ensembl; ENST00000351233.9; ENSP00000334070.7; ENSG00000163719.20. [Q8NCE2-3]
DR Ensembl; ENST00000353332.9; ENSP00000323462.8; ENSG00000163719.20. [Q8NCE2-2]
DR GeneID; 64419; -.
DR KEGG; hsa:64419; -.
DR MANE-Select; ENST00000296003.9; ENSP00000296003.5; NM_001077525.3; NP_001070993.1.
DR UCSC; uc003brz.4; human. [Q8NCE2-1]
DR CTD; 64419; -.
DR DisGeNET; 64419; -.
DR GeneCards; MTMR14; -.
DR HGNC; HGNC:26190; MTMR14.
DR HPA; ENSG00000163719; Low tissue specificity.
DR MalaCards; MTMR14; -.
DR MIM; 160150; phenotype.
DR MIM; 611089; gene.
DR neXtProt; NX_Q8NCE2; -.
DR OpenTargets; ENSG00000163719; -.
DR Orphanet; 169189; Autosomal dominant centronuclear myopathy.
DR PharmGKB; PA162396265; -.
DR VEuPathDB; HostDB:ENSG00000163719; -.
DR eggNOG; ENOG502QQ9R; Eukaryota.
DR GeneTree; ENSGT00390000018852; -.
DR HOGENOM; CLU_016325_2_0_1; -.
DR InParanoid; Q8NCE2; -.
DR OMA; QIVYLEY; -.
DR OrthoDB; 775284at2759; -.
DR PhylomeDB; Q8NCE2; -.
DR TreeFam; TF324044; -.
DR BioCyc; MetaCyc:HS08920-MON; -.
DR BRENDA; 3.1.3.64; 2681.
DR PathwayCommons; Q8NCE2; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR SignaLink; Q8NCE2; -.
DR BioGRID-ORCS; 64419; 10 hits in 1086 CRISPR screens.
DR ChiTaRS; MTMR14; human.
DR GeneWiki; MTMR14; -.
DR GenomeRNAi; 64419; -.
DR Pharos; Q8NCE2; Tbio.
DR PRO; PR:Q8NCE2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NCE2; protein.
DR Bgee; ENSG00000163719; Expressed in monocyte and 190 other tissues.
DR ExpressionAtlas; Q8NCE2; baseline and differential.
DR Genevisible; Q8NCE2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; TAS:Reactome.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; TAS:Reactome.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR CDD; cd13213; PH-GRAM_MTMR14; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR039802; MTMR14.
DR InterPro; IPR039803; MTMR14_PH-GRAM.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR13524; PTHR13524; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Disease variant;
KW Glycoprotein; Hydrolase; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..650
FT /note="Myotubularin-related protein 14"
FT /id="PRO_0000260214"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 479..538
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_021585"
FT VAR_SEQ 539..590
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.1"
FT /id="VSP_021586"
FT VARIANT 336
FT /note="R -> Q (in CNM1; may act as a phenotype modifier;
FT drastically reduced enzymatic activity; dbSNP:rs121434509)"
FT /evidence="ECO:0000269|PubMed:17008356"
FT /id="VAR_033370"
FT VARIANT 462
FT /note="Y -> C (in CNM1; may act as a disease modifier;
FT mutation found in a patient also carrying mutation Lys-368
FT in DNM2; reduced enzymatic activity; dbSNP:rs121434510)"
FT /evidence="ECO:0000269|PubMed:17008356"
FT /id="VAR_033371"
FT MUTAGEN 330
FT /note="C->S: Drastically reduced enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17008356"
FT CONFLICT 28
FT /note="G -> R (in Ref. 3; CAL38187)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="E -> G (in Ref. 3; CAL37928)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="R -> G (in Ref. 3; CAL38187)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="F -> S (in Ref. 2; BAC11211)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..406
FT /note="EEFS -> ALFA (in Ref. 5; AAS50151)"
FT /evidence="ECO:0000305"
FT CONFLICT 554..557
FT /note="GSWQ -> AAGM (in Ref. 5; AAS50151)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="S -> N (in Ref. 3; CAL37928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 72203 MW; C1B70E5140EF0716 CRC64;
MAGARAAAAA ASAGSSASSG NQPPQELGLG ELLEEFSRTQ YRAKDGSGTG GSKVERIEKR
CLELFGRDYC FSVIPNTNGD ICGHYPRHIV FLEYESSEKE KDTFESTVQV SKLQDLIHRS
KMARCRGRFV CPVILFKGKH ICRSATLAGW GELYGRSGYN YFFSGGADDA WADVEDVTEE
DCALRSGDTH LFDKVRGYDI KLLRYLSVKY ICDLMVENKK VKFGMNVTSS EKVDKAQRYA
DFTLLSIPYP GCEFFKEYKD RDYMAEGLIF NWKQDYVDAP LSIPDFLTHS LNIDWSQYQC
WDLVQQTQNY LKLLLSLVNS DDDSGLLVHC ISGWDRTPLF ISLLRLSLWA DGLIHTSLKP
TEILYLTVAY DWFLFGHMLV DRLSKGEEIF FFCFNFLKHI TSEEFSALKT QRRKSLPARD
GGFTLEDICM LRRKDRGSTT SLGSDFSLVM ESSPGATGSF TYEAVELVPA GAPTQAAWRK
SHSSSPQSVL WNRPQPSEDR LPSQQGLAEA RSSSSSSSNH SDNFFRMGSS PLEVPKPRSV
DHPLPGSSLS TDYGSWQMVT GCGSIQERAV LHTDSSLPFS FPDELPNSCL LAALSDRETR
LQEVRSAFLA AYSSTVGLRA VAPSPSGAIG GLLEQFARGV GLRSISSNAL
