NUCB1_HUMAN
ID NUCB1_HUMAN Reviewed; 461 AA.
AC Q02818; B2RD64; Q15838; Q7Z4J7; Q9BUR1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Nucleobindin-1;
DE AltName: Full=CALNUC;
DE Flags: Precursor;
GN Name=NUCB1; Synonyms=NUC;
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].
RX PubMed=1520323; DOI=10.1016/s0006-291x(05)81503-7;
RA Miura K., Titani K., Kurosawa Y., Kanai Y.;
RT "Molecular cloning of nucleobindin, a novel DNA-binding protein that
RT contains both a signal peptide and a leucine zipper structure.";
RL Biochem. Biophys. Res. Commun. 187:375-380(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 13-LEU-PRO-14 DELINS SER AND
RP GLN-399, AND SEQUENCE REVISION TO 299-300.
RC TISSUE=Placenta;
RX PubMed=8661046; DOI=10.1006/geno.1996.0263;
RA Miura K., Hirai M., Kanai Y., Kurosawa Y.;
RT "Organization of the human gene for nucleobindin (NUC) and its chromosomal
RT assignment to 19q13.2-q13.4.";
RL Genomics 34:181-186(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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].
RC TISSUE=Lung;
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 CHARACTERIZATION.
RX PubMed=7589456; DOI=10.1016/0014-5793(95)01031-9;
RA Mochizuki N., Hibi M., Kanai Y., Insel P.A.;
RT "Interaction of the protein nucleobindin with G alpha i2, as revealed by
RT the yeast two-hybrid system.";
RL FEBS Lett. 373:155-158(1995).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [10]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP PHOSPHORYLATION AT SER-86; THR-148 AND SER-369.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [13]
RP GBA MOTIF.
RX PubMed=30194280; DOI=10.1074/jbc.ra118.003580;
RA Maziarz M., Broselid S., DiGiacomo V., Park J.C., Luebbers A.,
RA Garcia-Navarrete L., Blanco-Canosa J.B., Baillie G.S., Garcia-Marcos M.;
RT "A biochemical and genetic discovery pipeline identifies PLCdelta4b as a
RT nonreceptor activator of heterotrimeric G-proteins.";
RL J. Biol. Chem. 293:16964-16983(2018).
RN [14]
RP STRUCTURE BY NMR OF 228-326, CALCIUM-BINDING, AND DOMAIN.
RX PubMed=15287731; DOI=10.1021/bi049310a;
RA de Alba E., Tjandra N.;
RT "Structural studies on the Ca2+-binding domain of human nucleobindin
RT (Calnuc).";
RL Biochemistry 43:10039-10049(2004).
CC -!- FUNCTION: Major calcium-binding protein of the Golgi which may have a
CC role in calcium homeostasis (By similarity). Acts as a non-receptor
CC guanine nucleotide exchange factor which binds to and activates alpha
CC subunits of guanine nucleotide-binding proteins (G proteins) (By
CC similarity). {ECO:0000250|UniProtKB:Q0P569,
CC ECO:0000250|UniProtKB:Q63083}.
CC -!- SUBUNIT: Interacts (via GBA motif) with guanine nucleotide-binding
CC protein G(i) alpha subunits GNAI1, GNAI2 and GNAI3 with higher affinity
CC for GNAI1 and GNAI3 than for GNAI2. Preferentially interacts with
CC inactive rather than active GNAI3. Interaction with GNAI3 is inhibited
CC when NUCB1 binds calcium, probably due to a conformational change which
CC renders the GBA motif inaccessible. {ECO:0000250|UniProtKB:Q63083}.
CC -!- INTERACTION:
CC Q02818; P05067: APP; NbExp=3; IntAct=EBI-2622179, EBI-77613;
CC Q02818; PRO_0000045603 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-2622179, EBI-6927928;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q63083}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q63083}; Lumenal side
CC {ECO:0000250|UniProtKB:Q63083}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q63083}. Secreted
CC {ECO:0000250|UniProtKB:Q63083}. Note=A small fraction of the protein
CC may be cytoplasmic. {ECO:0000250|UniProtKB:Q63083}.
CC -!- TISSUE SPECIFICITY: Expressed both in fetal and adult heart, lung,
CC liver, kidney and brain, and in adult skeletal muscle, placenta and
CC pancreas.
CC -!- DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+) and
CC fold upon Ca(2+) addition. {ECO:0000269|PubMed:15287731}.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000269|PubMed:30194280}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC -!- MISCELLANEOUS: Discovered as DNA-binding protein in the serum of lupus-
CC prone mice.
CC -!- SIMILARITY: Belongs to the nucleobindin family. {ECO:0000305}.
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DR EMBL; M96824; AAA36383.1; -; mRNA.
DR EMBL; U31342; AAB60431.1; -; Genomic_DNA.
DR EMBL; U31336; AAB60431.1; JOINED; Genomic_DNA.
DR EMBL; U31337; AAB60431.1; JOINED; Genomic_DNA.
DR EMBL; U31338; AAB60431.1; JOINED; Genomic_DNA.
DR EMBL; U31340; AAB60431.1; JOINED; Genomic_DNA.
DR EMBL; U31341; AAB60431.1; JOINED; Genomic_DNA.
DR EMBL; BT009828; AAP88830.1; -; mRNA.
DR EMBL; AK315422; BAG37811.1; -; mRNA.
DR EMBL; CH471177; EAW52411.1; -; Genomic_DNA.
DR EMBL; BC002356; AAH02356.1; -; mRNA.
DR CCDS; CCDS12740.1; -.
DR RefSeq; NP_006175.2; NM_006184.5.
DR RefSeq; XP_016882334.1; XM_017026845.1.
DR PDB; 1SNL; NMR; -; A=228-326.
DR PDBsum; 1SNL; -.
DR AlphaFoldDB; Q02818; -.
DR BMRB; Q02818; -.
DR SMR; Q02818; -.
DR BioGRID; 110978; 86.
DR IntAct; Q02818; 34.
DR MINT; Q02818; -.
DR STRING; 9606.ENSP00000385923; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR GuidetoPHARMACOLOGY; 2871; -.
DR GlyGen; Q02818; 9 sites, 7 O-linked glycans (4 sites).
DR iPTMnet; Q02818; -.
DR MetOSite; Q02818; -.
DR PhosphoSitePlus; Q02818; -.
DR BioMuta; NUCB1; -.
DR DMDM; 90110780; -.
DR EPD; Q02818; -.
DR jPOST; Q02818; -.
DR MassIVE; Q02818; -.
DR MaxQB; Q02818; -.
DR PaxDb; Q02818; -.
DR PeptideAtlas; Q02818; -.
DR PRIDE; Q02818; -.
DR ProteomicsDB; 58128; -.
DR Antibodypedia; 2173; 306 antibodies from 30 providers.
DR DNASU; 4924; -.
DR Ensembl; ENST00000405315.9; ENSP00000385923.3; ENSG00000104805.16.
DR Ensembl; ENST00000407032.5; ENSP00000385211.1; ENSG00000104805.16.
DR GeneID; 4924; -.
DR KEGG; hsa:4924; -.
DR MANE-Select; ENST00000405315.9; ENSP00000385923.3; NM_006184.6; NP_006175.2.
DR UCSC; uc002plb.5; human.
DR CTD; 4924; -.
DR DisGeNET; 4924; -.
DR GeneCards; NUCB1; -.
DR HGNC; HGNC:8043; NUCB1.
DR HPA; ENSG00000104805; Low tissue specificity.
DR MIM; 601323; gene.
DR neXtProt; NX_Q02818; -.
DR OpenTargets; ENSG00000104805; -.
DR PharmGKB; PA31825; -.
DR VEuPathDB; HostDB:ENSG00000104805; -.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00390000001927; -.
DR HOGENOM; CLU_031153_1_0_1; -.
DR InParanoid; Q02818; -.
DR OMA; QETDTNH; -.
DR OrthoDB; 1339224at2759; -.
DR PhylomeDB; Q02818; -.
DR TreeFam; TF323218; -.
DR PathwayCommons; Q02818; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q02818; -.
DR SIGNOR; Q02818; -.
DR BioGRID-ORCS; 4924; 275 hits in 1075 CRISPR screens.
DR ChiTaRS; NUCB1; human.
DR EvolutionaryTrace; Q02818; -.
DR GeneWiki; NUCB1; -.
DR GenomeRNAi; 4924; -.
DR Pharos; Q02818; Tchem.
DR PRO; PR:Q02818; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q02818; protein.
DR Bgee; ENSG00000104805; Expressed in stromal cell of endometrium and 195 other tissues.
DR ExpressionAtlas; Q02818; baseline and differential.
DR Genevisible; Q02818; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR040253; NUCB1.
DR InterPro; IPR040250; Nucleobindin.
DR PANTHER; PTHR19237; PTHR19237; 1.
DR PANTHER; PTHR19237:SF21; PTHR19237:SF21; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Coiled coil; Cytoplasm; DNA-binding; Glycoprotein;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250|UniProtKB:Q0P569"
FT CHAIN 27..461
FT /note="Nucleobindin-1"
FT /id="PRO_0000004162"
FT DOMAIN 240..275
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 292..327
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DNA_BIND 172..218
FT /evidence="ECO:0000255"
FT REGION 42..51
FT /note="O-glycosylated at one site"
FT REGION 193..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..321
FT /note="Binds to GNAI2 and GNAI3"
FT /evidence="ECO:0000250"
FT REGION 368..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 150..218
FT /evidence="ECO:0000255"
FT COILED 341..407
FT /evidence="ECO:0000255"
FT MOTIF 303..333
FT /note="GBA"
FT /evidence="ECO:0000269|PubMed:30194280"
FT COMPBIAS 193..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:15287731"
FT MOD_RES 86
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 148
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 369
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT VARIANT 13..14
FT /note="LP -> S"
FT /evidence="ECO:0000269|PubMed:8661046"
FT /id="VAR_012151"
FT VARIANT 338
FT /note="M -> V (in dbSNP:rs35456905)"
FT /id="VAR_061087"
FT VARIANT 399
FT /note="R -> Q (in dbSNP:rs200372110)"
FT /evidence="ECO:0000269|PubMed:8661046"
FT /id="VAR_012152"
FT CONFLICT 299..300
FT /note="HV -> QL (in Ref. 1; AAA36383)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="Q -> K (in Ref. 1; AAA36383 and 2; AAB60431)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..391
FT /note="QQ -> LL (in Ref. 1; AAA36383 and 2; AAB60431)"
FT /evidence="ECO:0000305"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:1SNL"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1SNL"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:1SNL"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:1SNL"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:1SNL"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:1SNL"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:1SNL"
SQ SEQUENCE 461 AA; 53879 MW; 913C4B87C2A644C5 CRC64;
MPPSGPRGTL LLLPLLLLLL LRAVLAVPLE RGAPNKEETP ATESPDTGLY YHRYLQEVID
VLETDGHFRE KLQAANAEDI KSGKLSRELD FVSHHVRTKL DELKRQEVSR LRMLLKAKMD
AEQDPNVQVD HLNLLKQFEH LDPQNQHTFE ARDLELLIQT ATRDLAQYDA AHHEEFKRYE
MLKEHERRRY LESLGEEQRK EAERKLEEQQ RRHREHPKVN VPGSQAQLKE VWEELDGLDP
NRFNPKTFFI LHDINSDGVL DEQELEALFT KELEKVYDPK NEEDDMREME EERLRMREHV
MKNVDTNQDR LVTLEEFLAS TQRKEFGDTG EGWETVEMHP AYTEEELRRF EEELAAREAE
LNAKAQRLSQ ETEALGRSQG RLEAQKRELQ QAVLHMEQRK QQQQQQQGHK APAAHPEGQL
KFHPDTDDVP VPAPAGDQKE VDTSEKKLLE RLPEVEVPQH L
