ID NELL2_MOUSE Reviewed; 819 AA. AC Q61220; Q80UM5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 18-SEP-2013, sequence version 3. DT 27-MAR-2024, entry version 177. DE RecName: Full=Protein kinase C-binding protein NELL2; DE AltName: Full=MEL91 protein; DE AltName: Full=NEL-like protein 2; DE Flags: Precursor; GN Name=Nell2 {ECO:0000312|MGI:MGI:1858510}; Synonyms=Mel91; 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]. RA Elkins D.A., Rossi J.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. 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]. RC STRAIN=C57BL/6J; 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 [5] RP FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH ROBO3, AND TISSUE RP SPECIFICITY. RX PubMed=26586761; DOI=10.1126/science.aad2615; RA Jaworski A., Tom I., Tong R.K., Gildea H.K., Koch A.W., Gonzalez L.C., RA Tessier-Lavigne M.; RT "Operational redundancy in axon guidance through the multifunctional RT receptor Robo3 and its ligand NELL2."; RL Science 350:961-965(2015). RN [6] RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND INTERACTION WITH ROS1. RX PubMed=32499443; DOI=10.1126/science.aay5134; RA Kiyozumi D., Noda T., Yamaguchi R., Tobita T., Matsumura T., Shimada K., RA Kodani M., Kohda T., Fujihara Y., Ozawa M., Yu Z., Miklossy G., RA Bohren K.M., Horie M., Okabe M., Matzuk M.M., Ikawa M.; RT "NELL2-mediated lumicrine signaling through OVCH2 is required for male RT fertility."; RL Science 368:1132-1135(2020). RN [7] RP FUNCTION, MUTAGENESIS OF ARG-451; TYR-453; ARG-455; ASP-480; TYR-481; RP LEU-501; PHE-503 AND VAL-512, SUBUNIT, AND INTERACTION WITH ROBO3. RX PubMed=32198364; DOI=10.1038/s41467-020-15211-1; RA Pak J.S., DeLoughery Z.J., Wang J., Acharya N., Park Y., Jaworski A., RA Ozkan E.; RT "NELL2-Robo3 complex structure reveals mechanisms of receptor activation RT for axon guidance."; RL Nat. Commun. 11:1489-1489(2020). RN [8] RP FUNCTION, SUBUNIT, AND INTERACTION WITH NICOL1. RX PubMed=37095084; DOI=10.1038/s41467-023-37984-x; RA Kiyozumi D., Shimada K., Chalick M., Emori C., Kodani M., Oura S., Noda T., RA Endo T., Matzuk M.M., Wreschner D.H., Ikawa M.; RT "A small secreted protein NICOL regulates lumicrine-mediated sperm RT maturation and male fertility."; RL Nat. Commun. 14:2354-2354(2023). CC -!- FUNCTION: Plays multiple roles in neural tissues, regulates neuronal CC proliferation, survival, differentiation, polarization, as well as axon CC guidance and synaptic functions. Plays an important role in axon CC development during neuronal differentiation through the MAPK CC intracellular signaling pathway (By similarity) (PubMed:32198364, CC PubMed:26586761). Via binding to its receptor ROBO3, plays a role in CC axon guidance, functioning as a repulsive axon guidance cue that CC contributes to commissural axon guidance to the midline CC (PubMed:32198364, PubMed:26586761). Required for neuron survival CC through the modulation of MAPK signaling pathways too. Involved in the CC regulation of hypothalamic GNRH secretion and the control of puberty CC (By similarity). {ECO:0000250|UniProtKB:Q62918, CC ECO:0000269|PubMed:26586761, ECO:0000269|PubMed:32198364}. CC -!- FUNCTION: Epididymal-secreted protein that signals through a ROS1- CC pathway to regulate the epididymal initial segment (IS) maturation, CC sperm maturation and male fertility. {ECO:0000269|PubMed:32499443, CC ECO:0000269|PubMed:37095084}. CC -!- SUBUNIT: Homotrimer (PubMed:32198364). Interacts with NICOL1; this CC interaction triggers epididymal differentiation (PubMed:37095084). CC Interacts (via EGF domains) with ROBO3 (via FN domains); binding to CC ROBO3 induces repulsive guidance cue for commissural axons CC (PubMed:26586761, PubMed:32198364). {ECO:0000269|PubMed:26586761, CC ECO:0000269|PubMed:32198364, ECO:0000269|PubMed:37095084}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32499443}. CC Note=Detected in the epididymal lumen. {ECO:0000269|PubMed:32499443}. CC -!- TISSUE SPECIFICITY: Expressed in brain and testis but not in epididymis CC (PubMed:32499443). Expressed in regions flanking the commissural axon CC trajectory, including the ventral horn (PubMed:26586761). CC {ECO:0000269|PubMed:26586761, ECO:0000269|PubMed:32499443}. CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc expressed in the presumptive motor CC column in the ventral horn. At 10.5 dpc, additional sites of expression CC include dorsal root ganglia, the dorsal mantle layer of the spinal CC cord, and a triangular population of cells close to the ventricle. CC Expression in cells forming ventral corridor persists at 11.5 dpc. CC {ECO:0000269|PubMed:26586761}. CC -!- DISRUPTION PHENOTYPE: Deficient male mice exhibit infertility, impaired CC binding of sperm to zona pellucida, and impaired sperm migration in CC female genital tract. Postnatal differentiation of the initial segment CC (IS) of the caput epididymis is completely abolished in Nell2 deficient CC males and continued throughout life. Ovch2 is not secreted and Adam3 is CC not processed into its mature form in cauda epididymal spermatozoa, CC leading to inability of spermatozoa to pass through the uterotubal CC junction and to bind to the zona pellucida. CC {ECO:0000269|PubMed:32499443}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator. CC {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; U59230; AAB02924.1; -; mRNA. DR EMBL; AC109198; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC163991; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC164402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC051968; AAH51968.1; -; mRNA. DR CCDS; CCDS27775.1; -. DR RefSeq; NP_001276582.1; NM_001289653.1. DR RefSeq; XP_006521226.1; XM_006521163.2. DR RefSeq; XP_011243995.1; XM_011245693.1. DR AlphaFoldDB; Q61220; -. DR SMR; Q61220; -. DR BioGRID; 207556; 3. DR IntAct; Q61220; 1. DR STRING; 10090.ENSMUSP00000131665; -. DR GlyConnect; 2634; 7 N-Linked glycans (2 sites). DR GlyCosmos; Q61220; 7 sites, 6 glycans. DR GlyGen; Q61220; 7 sites, 6 N-linked glycans (2 sites). DR iPTMnet; Q61220; -. DR PhosphoSitePlus; Q61220; -. DR SwissPalm; Q61220; -. DR PaxDb; 10090-ENSMUSP00000131665; -. DR PeptideAtlas; Q61220; -. DR ProteomicsDB; 252881; -. DR Antibodypedia; 25202; 227 antibodies from 27 providers. DR Ensembl; ENSMUST00000075275.3; ENSMUSP00000074751.3; ENSMUSG00000022454.18. DR Ensembl; ENSMUST00000166170.9; ENSMUSP00000131665.2; ENSMUSG00000022454.18. DR GeneID; 54003; -. DR KEGG; mmu:54003; -. DR UCSC; uc007xjq.2; mouse. DR AGR; MGI:1858510; -. DR CTD; 4753; -. DR MGI; MGI:1858510; Nell2. DR VEuPathDB; HostDB:ENSMUSG00000022454; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00810000125439; -. DR HOGENOM; CLU_006887_0_0_1; -. DR InParanoid; Q61220; -. DR OMA; TCGQFLE; -. DR OrthoDB; 5487at2759; -. DR PhylomeDB; Q61220; -. DR TreeFam; TF323325; -. DR BioGRID-ORCS; 54003; 1 hit in 79 CRISPR screens. DR ChiTaRS; Nell2; mouse. DR PRO; PR:Q61220; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q61220; Protein. DR Bgee; ENSMUSG00000022454; Expressed in dentate gyrus of hippocampal formation granule cell and 154 other cell types or tissues. DR ExpressionAtlas; Q61220; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0008201; F:heparin binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI. DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:UniProtKB. DR GO; GO:0046543; P:development of secondary female sexual characteristics; ISO:MGI. DR GO; GO:0009566; P:fertilization; IMP:UniProtKB. DR GO; GO:0022008; P:neurogenesis; ISO:MGI. DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB. DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:MGI. DR GO; GO:0040008; P:regulation of growth; ISO:MGI. DR CDD; cd00054; EGF_CA; 3. DR CDD; cd00110; LamG; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 6.20.200.20; -; 2. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR Gene3D; 2.10.25.10; Laminin; 6. DR InterPro; IPR013320; ConA-like_dom_sf. 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; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR024731; EGF_dom. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR048287; TSPN-like_N. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24042; NEL HOMOLOG; 1. DR PANTHER; PTHR24042:SF0; PROTEIN KINASE C-BINDING PROTEIN NELL2; 1. DR Pfam; PF12947; EGF_3; 1. DR Pfam; PF07645; EGF_CA; 3. DR Pfam; PF02210; Laminin_G_2; 1. DR Pfam; PF00093; VWC; 2. DR SMART; SM00181; EGF; 6. DR SMART; SM00179; EGF_CA; 5. DR SMART; SM00282; LamG; 1. DR SMART; SM00210; TSPN; 1. DR SMART; SM00214; VWC; 4. DR SMART; SM00215; VWC_out; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57603; FnI-like domain; 2. DR SUPFAM; SSF57184; Growth factor receptor domain; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 3. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 4. DR PROSITE; PS50026; EGF_3; 6. DR PROSITE; PS01187; EGF_CA; 3. DR PROSITE; PS01208; VWFC_1; 2. DR PROSITE; PS50184; VWFC_2; 3. DR Genevisible; Q61220; MM. PE 1: Evidence at protein level; KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Metal-binding; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CHAIN 25..819 FT /note="Protein kinase C-binding protein NELL2" FT /id="PRO_0000007667" FT DOMAIN 67..231 FT /note="Laminin G-like" FT DOMAIN 275..334 FT /note="VWFC 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 400..442 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 443..484 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 485..525 FT /note="EGF-like 3; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 526..556 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 558..604 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 605..640 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 701..759 FT /note="VWFC 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 444 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 446 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 462 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 463 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 466 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 558 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 559 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 561 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 577 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 578 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 581 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 605 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 606 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 608 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 624 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 625 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT BINDING 628 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CARBOHYD 56 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 296 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 520 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CARBOHYD 551 FT /note="O-linked (GlcNAc...) threonine" FT /evidence="ECO:0000250|UniProtKB:Q99435" FT CARBOHYD 618 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 638 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 404..416 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 410..425 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 427..441 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 447..460 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 454..469 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 471..483 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 489..502 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 496..511 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 513..524 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 528..538 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 532..544 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 546..555 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 562..575 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 569..584 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 586..603 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 609..622 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 616..631 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT DISULFID 633..639 FT /evidence="ECO:0000250|UniProtKB:Q99435" FT MUTAGEN 451 FT /note="R->A: Strong (120-fold) reduction of affinity FT towards ROBO3; when associated with A-453. Reduced axon FT repulsive activity; when associated with A-453." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 453 FT /note="Y->A: Strong (120-fold) reduction of affinity FT towards ROBO3; when associated with A-451. Reduced axon FT repulsive activity; when associated with A-453." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 455 FT /note="R->A: Mildly (2.4-fold) reduction of affinity FT towards ROBO3. Does not affect axon repulsive activity." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 480 FT /note="D->A: Strong (120-fold) reduction of affinity FT towards ROBO3; when associated with A-481." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 481 FT /note="Y->A: Strong (120-fold) reduction of affinity FT towards ROBO3; when associated with A-480." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 501 FT /note="L->A: Abolishes binding to ROBO3; when associated FT with A-503. Abolishes axon repulsive activity; when FT associated with A-503." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 503 FT /note="F->A: Abolishes binding to ROBO3; when associated FT with A-503. Abolishes axon repulsive activity; when FT associated with A-503." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 512 FT /note="V->A: Mildly (2.4-fold) reduced affinity for ROBO3. FT Does not affect axon repulsive activity." FT /evidence="ECO:0000269|PubMed:32198364" FT CONFLICT 81 FT /note="F -> L (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="S -> F (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 187 FT /note="P -> A (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="V -> A (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 423 FT /note="A -> V (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 470 FT /note="I -> V (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="N -> T (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 668 FT /note="C -> W (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="V -> D (in Ref. 1; AAB02924)" FT /evidence="ECO:0000305" SQ SEQUENCE 819 AA; 91432 MW; 530ECD363029571D CRC64; MHAMESRVLL RTFCVILGLG AVWGLGVDPS LQIDVLTELE LGESTDGVRQ VPGLHNGTKA FLFQESPRSI KASTATAERF FQKLRNKHEF TILVTLKQIH LNSGVILSIH HLDHRYLELE SSGHRNEIRL HYRSGTHRPH TEVFPYILAD AKWHKLSLAF SASHLILHID CNKIYERVVE MPSTDLPLGT TFWLGQRNNA HGYFKGIMQD VHVLVMPQGF IAQCPDLNRT CPTCNDFHGL VQKIMELQDI LSKTSAKLSR AEQRMNRLDQ CYCERTCTVK GTTYRESESW TDGCKNCTCL NGTIQCETLV CPAPDCPPKS APAYVDGKCC KECKSTCQFQ GRSYFEGERN TVYSSSGMCV LYECKDQTMK LVENIGCPPL DCPESHQIAL SHSCCKVCKG YDFCSEKHTC MENSVCRNLN DRAVCSCRDG FRALREDNAY CEDIDECAEG RHYCRENTMC VNTPGSFMCI CKTGYIRIDD YSCTEHDECL TNQHNCDENA LCFNTVGGHN CVCKPGYTGN GTTCKAFCKD GCRNGGACIA ANVCACPQGF TGPSCETDID ECSEGFVQCD SRANCINLPG WYHCECRDGY HDNGMFAPGG ESCEDIDECG TGRHSCTNDT ICFNLDGGYD CRCPHGKNCT GDCVHEGKVK HTGQIWVLEN DRCSVCSCQT GFVMCRRMVC DCENPTVDLS CCPECDPRLS SQCLHQNGET VYNSGDTWVQ DCRQCRCLQG EVDCWPLACP EVECEFSVLP ENECCPRCVT DPCQADTIRN DITKTCLDEM NVVRFTGSSW IKHGTECTLC QCKNGHLCCS VDPQCLQEL //