NELL2_HUMAN
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 03-AUG-2022, entry version 186.
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; P49639: HOXA1; NbExp=2; IntAct=EBI-946274, EBI-740785;
CC Q99435; Q9UIS9: MBD1; NbExp=2; IntAct=EBI-946274, EBI-867196;
CC Q99435; Q7Z417: NUFIP2; NbExp=2; IntAct=EBI-946274, EBI-1210753;
CC Q99435; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-946274, EBI-1752330;
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 Q99435-2; P37173: TGFBR2; NbExp=3; IntAct=EBI-17754404, EBI-296151;
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;
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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 AlphaFoldDB; Q99435; -.
DR SMR; Q99435; -.
DR BioGRID; 110828; 50.
DR DIP; DIP-49927N; -.
DR IntAct; Q99435; 44.
DR MINT; Q99435; -.
DR STRING; 9606.ENSP00000416341; -.
DR GlyGen; Q99435; 9 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q99435; -.
DR PhosphoSitePlus; Q99435; -.
DR BioMuta; NELL2; -.
DR DMDM; 2494289; -.
DR EPD; Q99435; -.
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; 205 antibodies from 27 providers.
DR DNASU; 4753; -.
DR Ensembl; ENST00000333837.8; ENSP00000327988.4; ENSG00000184613.11. [Q99435-2]
DR Ensembl; ENST00000395487.6; ENSP00000378866.2; ENSG00000184613.11. [Q99435-4]
DR Ensembl; ENST00000429094.7; ENSP00000390680.2; ENSG00000184613.11. [Q99435-1]
DR Ensembl; ENST00000437801.6; ENSP00000416341.2; ENSG00000184613.11. [Q99435-3]
DR Ensembl; ENST00000452445.6; ENSP00000394612.2; ENSG00000184613.11. [Q99435-1]
DR Ensembl; ENST00000549027.5; ENSP00000447927.1; ENSG00000184613.11. [Q99435-4]
DR GeneID; 4753; -.
DR KEGG; hsa:4753; -.
DR MANE-Select; ENST00000429094.7; ENSP00000390680.2; NM_001145108.2; NP_001138580.1.
DR UCSC; uc001rof.4; human. [Q99435-1]
DR CTD; 4753; -.
DR DisGeNET; 4753; -.
DR GeneCards; NELL2; -.
DR HGNC; HGNC:7751; NELL2.
DR HPA; ENSG00000184613; Tissue enhanced (brain, fallopian tube, retina).
DR MIM; 602320; gene.
DR neXtProt; NX_Q99435; -.
DR OpenTargets; ENSG00000184613; -.
DR PharmGKB; PA31553; -.
DR VEuPathDB; HostDB:ENSG00000184613; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00810000125439; -.
DR HOGENOM; CLU_006887_0_0_1; -.
DR InParanoid; Q99435; -.
DR OMA; RANCVNL; -.
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 SignaLink; Q99435; -.
DR BioGRID-ORCS; 4753; 9 hits in 1067 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 182 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; ISS:UniProtKB.
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:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB.
DR CDD; cd00110; LamG; 1.
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; IPR001007; VWF_dom.
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; 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; Reference proteome; Repeat;
KW 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"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 432..440
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:6POG"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 568..575
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:6POG"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:6POG"
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
