RP3A_HUMAN
ID RP3A_HUMAN Reviewed; 694 AA.
AC Q9Y2J0; B7Z3C3; Q96AE0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Rabphilin-3A;
DE AltName: Full=Exophilin-1;
GN Name=RPH3A; Synonyms=KIAA0985;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP INTERACTION WITH SNCA AND RAB3A.
RX PubMed=15207266; DOI=10.1016/j.nbd.2004.01.001;
RA Dalfo E., Barrachina M., Rosa J.L., Ambrosio S., Ferrer I.;
RT "Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse
RT Lewy body disease.";
RL Neurobiol. Dis. 16:92-97(2004).
CC -!- FUNCTION: Plays an essential role in docking and fusion steps of
CC regulated exocytosis (By similarity). At the presynaptic level, RPH3A
CC is recruited by RAB3A to the synaptic vesicle membrane in a GTP-
CC dependent manner where it modulates synaptic vesicle trafficking and
CC calcium-triggered neurotransmitter release (By similarity). In the
CC post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4
CC and regulates NMDA receptor stability. Also plays a role in the
CC exocytosis of arginine vasopressin hormone (By similarity).
CC {ECO:0000250|UniProtKB:P47709}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B
CC (By similarity). Interacts with RAB3A; this interaction recruits RPH3A
CC to synaptic vesicules (PubMed:15207266). Interacts (via C2B domain)
CC with SNAP25 (By similarity). Interacts with deubiquitinating enzyme
CC CAND1; this interaction results in the deubiquitination of RPH3A (By
CC similarity). Interacts with GRIN2A and DLG4; this ternary complex
CC regulates NMDA receptor composition at postsynaptic membranes (By
CC similarity). Interacts with SNCA (PubMed:15207266).
CC {ECO:0000250|UniProtKB:P47708, ECO:0000250|UniProtKB:P47709,
CC ECO:0000269|PubMed:15207266}.
CC -!- INTERACTION:
CC Q9Y2J0; O14936: CASK; NbExp=3; IntAct=EBI-1216802, EBI-1215506;
CC Q9Y2J0-2; O00194: RAB27B; NbExp=3; IntAct=EBI-16808141, EBI-10179046;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:P47709}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:P47709}. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:P47709}. Membrane
CC {ECO:0000250|UniProtKB:P47709}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2J0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2J0-2; Sequence=VSP_021016;
CC -!- DOMAIN: Binds calcium via the C2 domains. The calcium-bound C2 domains
CC mediate interactions with phospholipid bilayers (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by CAND1 to prevent its
CC degradation. {ECO:0000250|UniProtKB:P47709}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76829.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023202; BAA76829.2; ALT_INIT; mRNA.
DR EMBL; AK295696; BAH12159.1; -; mRNA.
DR EMBL; BC017259; AAH17259.1; -; mRNA.
DR CCDS; CCDS31904.1; -. [Q9Y2J0-2]
DR CCDS; CCDS44979.1; -. [Q9Y2J0-1]
DR RefSeq; NP_001137326.1; NM_001143854.1. [Q9Y2J0-1]
DR RefSeq; NP_001334881.1; NM_001347952.1. [Q9Y2J0-1]
DR RefSeq; NP_001334882.1; NM_001347953.1. [Q9Y2J0-1]
DR RefSeq; NP_001334883.1; NM_001347954.1. [Q9Y2J0-1]
DR RefSeq; NP_055769.2; NM_014954.3. [Q9Y2J0-2]
DR AlphaFoldDB; Q9Y2J0; -.
DR SMR; Q9Y2J0; -.
DR BioGRID; 116560; 25.
DR IntAct; Q9Y2J0; 12.
DR MINT; Q9Y2J0; -.
DR STRING; 9606.ENSP00000374036; -.
DR iPTMnet; Q9Y2J0; -.
DR PhosphoSitePlus; Q9Y2J0; -.
DR SwissPalm; Q9Y2J0; -.
DR BioMuta; RPH3A; -.
DR DMDM; 13878745; -.
DR MassIVE; Q9Y2J0; -.
DR PaxDb; Q9Y2J0; -.
DR PeptideAtlas; Q9Y2J0; -.
DR PRIDE; Q9Y2J0; -.
DR ProteomicsDB; 85809; -. [Q9Y2J0-1]
DR ProteomicsDB; 85810; -. [Q9Y2J0-2]
DR Antibodypedia; 996; 276 antibodies from 33 providers.
DR DNASU; 22895; -.
DR Ensembl; ENST00000389385.9; ENSP00000374036.4; ENSG00000089169.15. [Q9Y2J0-1]
DR Ensembl; ENST00000415485.7; ENSP00000405357.3; ENSG00000089169.15. [Q9Y2J0-1]
DR Ensembl; ENST00000543106.6; ENSP00000440384.2; ENSG00000089169.15. [Q9Y2J0-1]
DR Ensembl; ENST00000551052.5; ENSP00000448297.1; ENSG00000089169.15. [Q9Y2J0-2]
DR GeneID; 22895; -.
DR KEGG; hsa:22895; -.
DR MANE-Select; ENST00000389385.9; ENSP00000374036.4; NM_001143854.2; NP_001137326.1.
DR UCSC; uc001tty.4; human. [Q9Y2J0-1]
DR CTD; 22895; -.
DR DisGeNET; 22895; -.
DR GeneCards; RPH3A; -.
DR HGNC; HGNC:17056; RPH3A.
DR HPA; ENSG00000089169; Tissue enriched (brain).
DR MIM; 612159; gene.
DR neXtProt; NX_Q9Y2J0; -.
DR OpenTargets; ENSG00000089169; -.
DR PharmGKB; PA134886118; -.
DR VEuPathDB; HostDB:ENSG00000089169; -.
DR eggNOG; KOG1013; Eukaryota.
DR GeneTree; ENSGT00940000157468; -.
DR HOGENOM; CLU_011461_2_0_1; -.
DR InParanoid; Q9Y2J0; -.
DR OMA; TREIWLC; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; Q9Y2J0; -.
DR TreeFam; TF351844; -.
DR PathwayCommons; Q9Y2J0; -.
DR SignaLink; Q9Y2J0; -.
DR BioGRID-ORCS; 22895; 7 hits in 1062 CRISPR screens.
DR ChiTaRS; RPH3A; human.
DR GeneWiki; RPH3A; -.
DR GenomeRNAi; 22895; -.
DR Pharos; Q9Y2J0; Tbio.
DR PRO; PR:Q9Y2J0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y2J0; protein.
DR Bgee; ENSG00000089169; Expressed in right frontal lobe and 134 other tissues.
DR ExpressionAtlas; Q9Y2J0; baseline and differential.
DR Genevisible; Q9Y2J0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030141; C:secretory granule; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042301; F:phosphate ion binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008430; F:selenium binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR028698; RPH3A.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45729; PTHR45729; 1.
DR PANTHER; PTHR45729:SF3; PTHR45729:SF3; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection;
KW Cytoplasmic vesicle; Lipid-binding; Membrane; Metal-binding; Methylation;
KW Phosphoprotein; Postsynaptic cell membrane; Protein transport;
KW Reference proteome; Repeat; Synapse; Transport; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..694
FT /note="Rabphilin-3A"
FT /id="PRO_0000190227"
FT DOMAIN 44..160
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 392..514
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 550..683
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 92..148
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT MOD_RES 226
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT VAR_SEQ 24..28
FT /note="NDKEQ -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021016"
SQ SEQUENCE 694 AA; 76872 MW; BD9C43F306A04D69 CRC64;
MTDTVFSNSS NRWMYPSDRP LQSNDKEQLQ AGWSVHPGGQ PDRQRKQEEL TDEEKEIINR
VIARAEKMEE MEQERIGRLV DRLENMRKNV AGDGVNRCIL CGEQLGMLGS ACVVCEDCKK
NVCTKCGVET NNRLHSVWLC KICIEQREVW KRSGAWFFKG FPKQVLPQPM PIKKTKPQQP
VSEPAAPEQP APEPKHPARA PARGDSEDRR GPGQKTGPDP ASAPGRGNYG PPVRRASEAR
MSSSSRDSES WDHSGGAGDS SRSPAGLRRA NSVQASRPAP GSVQSPAPPQ PGQPGTPGGS
RPGPGPAGRF PDQKPEVAPS DPGTTAPPRE ERTGGVGGYP AVGAREDRMS HPSGPYSQAS
AAAPQPAAAR QPPPPEEEEE EANSYDSDEA TTLGALEFSL LYDQDNSSLQ CTIIKAKGLK
PMDSNGLADP YVKLHLLPGA SKSNKLRTKT LRNTRNPIWN ETLVYHGITD EDMQRKTLRI
SVCDEDKFGH NEFIGETRFS LKKLKPNQRK NFNICLERVI PMKRAGTTGS ARGMALYEEE
QVERVGDIEE RGKILVSLMY STQQGGLIVG IIRCVHLAAM DANGYSDPFV KLWLKPDMGK
KAKHKTQIKK KTLNPEFNEE FFYDIKHSDL AKKSLDISVW DYDIGKSNDY IGGCQLGISA
KGERLKHWYE CLKNKDKKIE RWHQLQNENH VSSD
