ID NELL2_HUMAN Reviewed; 816 AA. AC Q99435; B7Z2U7; B7Z5Q4; B7Z9J5; B7Z9U3; Q96JS2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 12-AUG-2020, entry version 177. DE RecName: Full=Protein kinase C-binding protein NELL2; DE AltName: Full=NEL-like protein 2; DE AltName: Full=Nel-related protein 2; DE Flags: Precursor; GN Name=NELL2; Synonyms=NRP2; 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 1). RC TISSUE=Brain; RX PubMed=8975702; DOI=10.1006/geno.1996.0628; RA Watanabe T.K., Katagiri T., Suzuki M., Shimizu F., Fujiwara T., RA Kanemoto N., Nakamura Y., Hirai Y., Maekawa H., Takahashi E.; RT "Cloning and characterization of two novel human cDNAs (NELL1 and NELL2) RT encoding proteins with six EGF-like repeats."; RL Genomics 38:273-276(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Brain; RA Yoshimoto M., Yazaki M., Takayama K., Matsumoto K.; RT "Biological functions of a novel human gene, hucep-12, which is RT specifically expressed in the central nervous system."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Amygdala, Brain, and Hippocampus; 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 GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Duodenum; 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 PROTEIN SEQUENCE OF 22-36 (ISOFORM 1). RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). CC -!- FUNCTION: Required for neuron survival through the modulation of MAPK CC pathways (By similarity). Involved in the regulation of hypothalamic CC GNRH secretion and the control of puberty (By similarity). CC {ECO:0000250|UniProtKB:Q62918}. CC -!- SUBUNIT: Homotrimer. Binds to PKC beta-1 (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q99435; Q5VTD9: GFI1B; NbExp=2; IntAct=EBI-946274, EBI-946212; CC Q99435-1; Q96MS0: ROBO3; NbExp=3; IntAct=EBI-16185191, EBI-1220465; CC Q99435-2; P49639: HOXA1; NbExp=3; IntAct=EBI-17754404, EBI-740785; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q62918}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q99435-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99435-2; Sequence=VSP_043801; CC Name=3; CC IsoId=Q99435-3; Sequence=VSP_043802; CC Name=4; CC IsoId=Q99435-4; Sequence=VSP_043869; 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; D83018; BAA11681.1; -; mRNA. DR EMBL; D89629; BAB46925.1; -; mRNA. DR EMBL; AK295125; BAH11983.1; -; mRNA. DR EMBL; AK299277; BAH12990.1; -; mRNA. DR EMBL; AK315960; BAH14331.1; -; mRNA. DR EMBL; AK316058; BAH14429.1; -; mRNA. DR EMBL; AC018923; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025253; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079033; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079825; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471111; EAW57873.1; -; Genomic_DNA. DR EMBL; BC020544; AAH20544.1; -; mRNA. DR CCDS; CCDS44863.1; -. [Q99435-3] DR CCDS; CCDS44864.1; -. [Q99435-4] DR CCDS; CCDS53781.1; -. [Q99435-2] DR CCDS; CCDS8746.1; -. [Q99435-1] DR RefSeq; NP_001138579.1; NM_001145107.1. [Q99435-3] DR RefSeq; NP_001138580.1; NM_001145108.1. [Q99435-1] DR RefSeq; NP_001138581.1; NM_001145109.1. [Q99435-4] DR RefSeq; NP_001138582.1; NM_001145110.1. [Q99435-2] DR RefSeq; NP_006150.1; NM_006159.2. [Q99435-1] DR RefSeq; XP_005268962.1; XM_005268905.3. [Q99435-1] DR RefSeq; XP_011536698.1; XM_011538396.1. [Q99435-1] DR PDB; 6POG; X-ray; 2.75 A; B=397-638. DR PDBsum; 6POG; -. DR SMR; Q99435; -. DR BioGRID; 110828; 37. DR DIP; DIP-49927N; -. DR IntAct; Q99435; 39. DR MINT; Q99435; -. DR STRING; 9606.ENSP00000416341; -. DR GlyGen; Q99435; 7 sites. DR iPTMnet; Q99435; -. DR PhosphoSitePlus; Q99435; -. DR BioMuta; NELL2; -. DR DMDM; 2494289; -. DR MassIVE; Q99435; -. DR PaxDb; Q99435; -. DR PeptideAtlas; Q99435; -. DR PRIDE; Q99435; -. DR ProteomicsDB; 78262; -. [Q99435-1] DR ProteomicsDB; 78263; -. [Q99435-2] DR ProteomicsDB; 78264; -. [Q99435-3] DR ProteomicsDB; 78265; -. [Q99435-4] DR Antibodypedia; 25202; 187 antibodies. DR DNASU; 4753; -. DR Ensembl; ENST00000333837; ENSP00000327988; ENSG00000184613. [Q99435-2] DR Ensembl; ENST00000395487; ENSP00000378866; ENSG00000184613. [Q99435-4] DR Ensembl; ENST00000429094; ENSP00000390680; ENSG00000184613. [Q99435-1] DR Ensembl; ENST00000437801; ENSP00000416341; ENSG00000184613. [Q99435-3] DR Ensembl; ENST00000452445; ENSP00000394612; ENSG00000184613. [Q99435-1] DR Ensembl; ENST00000549027; ENSP00000447927; ENSG00000184613. [Q99435-4] DR GeneID; 4753; -. DR KEGG; hsa:4753; -. DR UCSC; uc001rof.4; human. [Q99435-1] DR CTD; 4753; -. DR DisGeNET; 4753; -. DR EuPathDB; HostDB:ENSG00000184613.10; -. DR GeneCards; NELL2; -. DR HGNC; HGNC:7751; NELL2. DR HPA; ENSG00000184613; Tissue enhanced (blood, brain, fallopian tube). DR MIM; 602320; gene. DR neXtProt; NX_Q99435; -. DR OpenTargets; ENSG00000184613; -. DR PharmGKB; PA31553; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00810000125439; -. DR HOGENOM; CLU_006887_0_0_1; -. DR InParanoid; Q99435; -. DR OMA; NCPESQQ; -. DR OrthoDB; 767046at2759; -. DR PhylomeDB; Q99435; -. DR TreeFam; TF323325; -. DR PathwayCommons; Q99435; -. DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO. DR BioGRID-ORCS; 4753; 6 hits in 873 CRISPR screens. DR ChiTaRS; NELL2; human. DR GeneWiki; NELL2; -. DR GenomeRNAi; 4753; -. DR Pharos; Q99435; Tbio. DR PRO; PR:Q99435; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q99435; protein. DR Bgee; ENSG00000184613; Expressed in middle temporal gyrus and 218 other tissues. DR ExpressionAtlas; Q99435; baseline and differential. DR Genevisible; Q99435; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central. DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR001007; VWF_dom. DR Pfam; PF07645; EGF_CA; 4. 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; 3. DR SMART; SM00215; VWC_out; 2. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF57184; SSF57184; 1. 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Direct protein sequencing; KW Disulfide bond; EGF-like domain; Glycoprotein; Polymorphism; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..21 FT CHAIN 22..816 FT /note="Protein kinase C-binding protein NELL2" FT /id="PRO_0000007666" FT DOMAIN 64..228 FT /note="Laminin G-like" FT DOMAIN 272..331 FT /note="VWFC 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 397..439 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 440..481 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 482..522 FT /note="EGF-like 3; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 523..553 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 555..601 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 602..637 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 638..693 FT /note="VWFC 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 698..756 FT /note="VWFC 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 225 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 293 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 298 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 517 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 615 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 635 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 401..413 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 407..422 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 424..438 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 444..457 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 451..466 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 468..480 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 486..499 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 493..508 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 510..521 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 525..535 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 529..541 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 543..552 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 559..572 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 566..581 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 583..600 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 606..619 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 613..628 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 630..636 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VAR_SEQ 1..18 FT /note="MESRVLLRTFCLIFGLGA -> METGLGAPLFKAWLLIS (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_043869" FT VAR_SEQ 1 FT /note="M -> MSIRRLLILILKIGRRWTELIRTM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043801" FT VAR_SEQ 1 FT /note="M -> MGFPPLLKGQASATRSSLASCSWVVFFLSCLSRHAPEIEGGRRWTEL FT IRTM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043802" FT VARIANT 5 FT /note="V -> I (in dbSNP:rs2658973)" FT /id="VAR_048987" FT VARIANT 347 FT /note="N -> D (in dbSNP:rs17574839)" FT /id="VAR_048988" FT VARIANT 631 FT /note="P -> L (in dbSNP:rs1050710)" FT /id="VAR_048989" FT CONFLICT 353 FT /note="S -> P (in Ref. 3; BAH12990)" FT /evidence="ECO:0000305" FT CONFLICT 454 FT /note="N -> D (in Ref. 3; BAH12990)" FT /evidence="ECO:0000305" FT CONFLICT 489 FT /note="N -> D (in Ref. 3; BAH14331)" FT /evidence="ECO:0000305" FT CONFLICT 636 FT /note="C -> S (in Ref. 3; BAH14331)" FT /evidence="ECO:0000305" SQ SEQUENCE 816 AA; 91346 MW; 89370B987DC7A324 CRC64; MESRVLLRTF CLIFGLGAVW GLGVDPSLQI DVLTELELGE STTGVRQVPG LHNGTKAFLF QDTPRSIKAS TATAEQFFQK LRNKHEFTIL VTLKQTHLNS GVILSIHHLD HRYLELESSG HRNEVRLHYR SGSHRPHTEV FPYILADDKW HKLSLAISAS HLILHIDCNK IYERVVEKPS TDLPLGTTFW LGQRNNAHGY FKGIMQDVQL LVMPQGFIAQ CPDLNRTCPT CNDFHGLVQK IMELQDILAK TSAKLSRAEQ RMNRLDQCYC ERTCTMKGTT YREFESWIDG CKNCTCLNGT IQCETLICPN PDCPLKSALA YVDGKCCKEC KSICQFQGRT YFEGERNTVY SSSGVCVLYE CKDQTMKLVE SSGCPALDCP ESHQITLSHS CCKVCKGYDF CSERHNCMEN SICRNLNDRA VCSCRDGFRA LREDNAYCED IDECAEGRHY CRENTMCVNT PGSFMCICKT GYIRIDDYSC TEHDECITNQ HNCDENALCF NTVGGHNCVC KPGYTGNGTT CKAFCKDGCR NGGACIAANV CACPQGFTGP SCETDIDECS DGFVQCDSRA NCINLPGWYH CECRDGYHDN GMFSPSGESC EDIDECGTGR HSCANDTICF NLDGGYDCRC PHGKNCTGDC IHDGKVKHNG QIWVLENDRC SVCSCQNGFV MCRRMVCDCE NPTVDLFCCP ECDPRLSSQC LHQNGETLYN SGDTWVQNCQ QCRCLQGEVD CWPLPCPDVE CEFSILPENE CCPRCVTDPC QADTIRNDIT KTCLDEMNVV RFTGSSWIKH GTECTLCQCK NGHICCSVDP QCLQEL //