ID   NELL2_RAT               Reviewed;         819 AA.
AC   Q62918; A1E5S7; C8CB44; Q561K2; Q8R417;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Protein kinase C-binding protein NELL2;
DE   AltName: Full=NEL-like protein 2;
DE   Flags: Precursor;
GN   Name=Nell2; Synonyms=Nel;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=10548494; DOI=10.1006/bbrc.1999.1638;
RA   Kuroda S., Oyasu M., Kawakami M., Kanayama N., Tanizawa K., Saito N.,
RA   Abe T., Matsuhashi S., Ting K.;
RT   "Biochemical characterization and expression analysis of neural
RT   thrombospondin-1-like proteins NELL1 and NELL2.";
RL   Biochem. Biophys. Res. Commun. 265:79-86(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Lee B.J., Kim H., Ha C.M., Choi E.J., Jeon J., Kim C., Park S.K.,
RA   Kang S.S., Kim K.;
RT   "Ontogeny and a possible role of a novel epidermal growth factor-like
RT   repeat domain-containing protein, NELL2 in the rat brain.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND SUBCELLULAR LOCATION (ISOFORM
RP   3).
RX   PubMed=19931511; DOI=10.1016/j.bbrc.2009.11.092;
RA   Kim D.G., Hwang E.M., Yoo J.C., Kim E., Park N., Rhee S., Ha C.M.,
RA   Hong S.G., Park J.Y.;
RT   "Identification and characterization of a truncated isoform of NELL2.";
RL   Biochem. Biophys. Res. Commun. 391:529-534(2010).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2),
RP   TISSUE SPECIFICITY (ISOFORM 2), AND INTERACTION WITH PRKCB (ISOFORM 2).
RX   PubMed=17196548; DOI=10.1016/j.bbrc.2006.12.115;
RA   Hwang E.M., Kim D.G., Lee B.J., Choi J., Kim E., Park N., Kang D., Han J.,
RA   Choi W.S., Hong S.G., Park J.Y.;
RT   "Alternative splicing generates a novel non-secretable cytosolic isoform of
RT   NELL2.";
RL   Biochem. Biophys. Res. Commun. 353:805-811(2007).
RN   [7]
RP   PHOSPHORYLATION, SUBUNIT, AND INTERACTION WITH PRKCB.
RX   PubMed=10600492; DOI=10.1006/bbrc.1999.1753;
RA   Kuroda S., Tanizawa K.;
RT   "Involvement of epidermal growth factor-like domain of NELL proteins in the
RT   novel protein-protein interaction with protein kinase C.";
RL   Biochem. Biophys. Res. Commun. 265:752-757(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=12941464; DOI=10.1016/s0169-328x(03)00256-0;
RA   Aihara K., Kuroda S., Kanayama N., Matsuyama S., Tanizawa K., Horie M.;
RT   "A neuron-specific EGF family protein, NELL2, promotes survival of neurons
RT   through mitogen-activated protein kinases.";
RL   Brain Res. Mol. Brain Res. 116:86-93(2003).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=18547942; DOI=10.1159/000139579;
RA   Ha C.M., Choi J., Choi E.J., Costa M.E., Lee B.J., Ojeda S.R.;
RT   "NELL2, a neuron-specific EGF-like protein, is selectively expressed in
RT   glutamatergic neurons and contributes to the glutamatergic control of GnRH
RT   neurons at puberty.";
RL   Neuroendocrinology 88:199-211(2008).
RN   [10]
RP   FUNCTION (ISOFORM 2), INTERACTION WITH PRKCB (ISOFORM 2), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=25450684; DOI=10.1016/j.bbrc.2014.10.110;
RA   Lee D.Y., Kim E., Lee Y.S., Ryu H., Park J.Y., Hwang E.M.;
RT   "The cytosolic splicing variant of NELL2 inhibits PKCbeta1 in glial
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 454:459-464(2014).
RN   [11]
RP   FUNCTION.
RX   PubMed=32597395; DOI=10.14348/molcells.2020.0032;
RA   Kim H.R., Kim D.H., An J.Y., Kang D., Park J.W., Hwang E.M., Seo E.J.,
RA   Jang I.H., Ha C.M., Lee B.J.;
RT   "NELL2 Function in Axon Development of Hippocampal Neurons.";
RL   Mol. Cells 43:581-589(2020).
CC   -!- FUNCTION: Plays multiple roles In neural tissues, regulates neuronal
CC       proliferation, survival, differentiation, polarization, as well as axon
CC       guidance and synaptic functions (PubMed:32597395, PubMed:12941464,
CC       PubMed:18547942). Plays an important role in axon development during
CC       neuronal differentiation through the MAPK intracellular signaling
CC       pathway (PubMed:32597395). Via binding to its receptor ROBO3, plays a
CC       role in axon guidance, functioning as a repulsive axon guidance cue
CC       that contributes to commissural axon guidance to the midline (By
CC       similarity). Required for neuron survival through the modulation of
CC       MAPK signaling pathways too (PubMed:12941464). Involved in the
CC       regulation of hypothalamic GNRH secretion and the control of puberty
CC       (PubMed:18547942). {ECO:0000250|UniProtKB:Q61220,
CC       ECO:0000269|PubMed:12941464, ECO:0000269|PubMed:18547942,
CC       ECO:0000269|PubMed:32597395}.
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:0000250|UniProtKB:Q61220}.
CC   -!- FUNCTION: [Isoform 2]: Acts as an endogenous inhibitor of PRKCB in
CC       glia. {ECO:0000269|PubMed:25450684}.
CC   -!- SUBUNIT: Homotrimer (PubMed:10548494). Binds to PRKCB (PubMed:10600492,
CC       PubMed:12941464, PubMed:25450684). Interacts with NICOL1; this
CC       interaction triggers epididymal differentiation (By similarity).
CC       {ECO:0000250|UniProtKB:Q61220, ECO:0000269|PubMed:10548494,
CC       ECO:0000269|PubMed:10600492, ECO:0000269|PubMed:12941464,
CC       ECO:0000269|PubMed:25450684}.
CC   -!- SUBUNIT: [Isoform 2]: Binds to PRKCB. {ECO:0000269|PubMed:17196548,
CC       ECO:0000269|PubMed:25450684}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC       {ECO:0000269|PubMed:10548494, ECO:0000269|PubMed:17196548,
CC       ECO:0000269|PubMed:18547942}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:17196548}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC       {ECO:0000269|PubMed:19931511}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q62918-1; Sequence=Displayed;
CC       Name=2; Synonyms=cNELL2 {ECO:0000303|PubMed:17196548};
CC         IsoId=Q62918-2; Sequence=VSP_062042;
CC       Name=3; Synonyms=NELL2-Tsp {ECO:0000303|PubMed:19931511};
CC         IsoId=Q62918-3; Sequence=VSP_062043;
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed (PubMed:17196548).
CC       Expressed in cortical astrocytes but not in neuron (PubMed:25450684).
CC       {ECO:0000269|PubMed:17196548, ECO:0000269|PubMed:25450684}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in brain (PubMed:18547942). High
CC       expression is observed in telencephalic and diencephalic glutamatergic
CC       neurons, while no expression is found in GABAergic and GNRH neurons
CC       (PubMed:18547942). {ECO:0000269|PubMed:18547942}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72245.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAL89577.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ABL61253.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ACU68930.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U48245; AAC72245.1; ALT_INIT; mRNA.
DR   EMBL; AY089719; AAL89577.1; ALT_INIT; mRNA.
DR   EMBL; EF110908; ABL61253.1; ALT_INIT; mRNA.
DR   EMBL; GQ376510; ACU68930.1; ALT_INIT; mRNA.
DR   EMBL; AABR07058759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07058770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093617; AAH93617.1; -; mRNA.
DR   RefSeq; NP_112332.2; NM_031070.2. [Q62918-1]
DR   RefSeq; XP_008764019.1; XM_008765797.2.
DR   RefSeq; XP_008764020.1; XM_008765798.2. [Q62918-1]
DR   AlphaFoldDB; Q62918; -.
DR   SMR; Q62918; -.
DR   STRING; 10116.ENSRNOP00000008985; -.
DR   GlyCosmos; Q62918; 7 sites, No reported glycans.
DR   GlyGen; Q62918; 7 sites.
DR   PhosphoSitePlus; Q62918; -.
DR   PaxDb; Q62918; -.
DR   Ensembl; ENSRNOT00000008985.8; ENSRNOP00000008985.5; ENSRNOG00000006235.8. [Q62918-1]
DR   Ensembl; ENSRNOT00065028985; ENSRNOP00065022951; ENSRNOG00065017359.
DR   Ensembl; ENSRNOT00065028999; ENSRNOP00065022964; ENSRNOG00065017359. [Q62918-1]
DR   GeneID; 81734; -.
DR   KEGG; rno:81734; -.
DR   UCSC; RGD:620999; rat. [Q62918-1]
DR   AGR; RGD:620999; -.
DR   CTD; 4753; -.
DR   RGD; 620999; Nell2.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00810000125439; -.
DR   HOGENOM; CLU_006887_0_0_1; -.
DR   InParanoid; Q62918; -.
DR   OrthoDB; 5487at2759; -.
DR   PhylomeDB; Q62918; -.
DR   TreeFam; TF323325; -.
DR   PRO; PR:Q62918; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000006235; Expressed in frontal cortex and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
DR   GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
DR   GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:UniProtKB.
DR   GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IDA:UniProtKB.
DR   GO; GO:0046887; P:positive regulation of hormone secretion; IMP:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; IDA:RGD.
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; 3.
DR   SMART; SM00215; VWC_out; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57603; FnI-like domain; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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   Alternative splicing; Calcium; Cytoplasm; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Metal-binding; 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_0000007668"
FT   DOMAIN          58..231
FT                   /note="Laminin G-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
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          641..696
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          701..759
FT                   /note="VWFC 3"
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   VAR_SEQ         22..64
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_062042"
FT   VAR_SEQ         262..819
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_062043"
FT   CONFLICT        282
FT                   /note="T -> A (in Ref. 1; AAC72245 and 2; AAL89577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        533
FT                   /note="R -> K (in Ref. 1; AAC72245)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        676
FT                   /note="R -> Q (in Ref. 1; AAC72245)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        719
FT                   /note="V -> A (in Ref. 1; AAC72245)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        730
FT                   /note="G -> E (in Ref. 1; AAC72245)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   819 AA;  91334 MW;  EF6A1B98F1C43202 CRC64;
     MHAMESRVLL RTFCVILGLE AVWGLGVDPS LQIDVLSELE LGESTAGVRQ VPGLHNGTKA
     FLFQDSPRSI KAPIATAERF FQKLRNKHEF TILVTLKQIH LNSGVILSIH HLDHRYLELE
     SSGHRNEIRL HYRSGTHRPH TEVFPYILAD AKWHKLSLAF SASHLILHID CNKIYERVVE
     MPSTDLPLGT TFWLGQRNNA HGYFKGIMQD VQLLVMPQGF IAQCPDLNRT CPTCNDFHGL
     VQKIMELQDI LSKTSAKLSR AEQRMNRLDQ CYCERTCTMK GTTYREFESW TDGCKNCTCL
     NGTIQCETLV CPAPDCPAKS APAYVDGKCC KECKSTCQFQ GRSYFEGERS TVFSASGMCV
     LYECKDQTMK LVENAGCPAL DCPESHQIAL SHSCCKVCKG YDFCSEKHTC MENSVCRNLN
     DRAVCSCRDG FRALREDNAY CEDIDECAEG RHYCRENTMC VNTPGSFLCI CQTGYIRIDD
     YSCTEHDECL TNQHNCDENA LCFNTVGGHN CVCKPGYTGN GTTCKAFCKD GCRNGGACIA
     ANVCACPQGF TGPSCETDID ECSEGFVQCD SRANCINLPG WYHCECRDGY HDNGMFAPGG
     ESCEDIDECG TGRHSCANDT ICFNLDGGYD CRCPHGKNCT GDCVHDGKVK HNGQIWVLEN
     DRCSVCSCQT GFVMCRRMVC DCENPTVDLS CCPECDPRLS SQCLHQNGET VYNSGDTWVQ
     DCRQCRCLQG EVDCWPLACP EVECEFSVLP ENECCPRCVT DPCQADTIRN DITKTCLDEM
     NVVRFTGSSW IKHGTECTLC QCKNGHVCCS VDPQCLQEL
//