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CRNN_HUMAN
ID   CRNN_HUMAN              Reviewed;         495 AA.
AC   Q9UBG3; B2RE60; Q8N613;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Cornulin;
DE   AltName: Full=53 kDa putative calcium-binding protein;
DE   AltName: Full=53 kDa squamous epithelial-induced stress protein;
DE   AltName: Full=58 kDa heat shock protein;
DE   AltName: Full=Squamous epithelial heat shock protein 53;
DE   AltName: Full=Tumor-related protein;
GN   Name=CRNN;
GN   Synonyms=C1orf10 {ECO:0000303|PubMed:30009832}, DRC1, PDRC1,
GN   SEP53 {ECO:0000303|PubMed:30009832};
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal esophagus;
RX   PubMed=11056050; DOI=10.1006/geno.2000.6344;
RA   Xu Z., Wang M.-R., Xu X., Cai Y., Han Y.-L., Wu K.-M., Wang J., Chen B.-S.,
RA   Wang X.-Q., Wu M.;
RT   "Novel human esophagus-specific gene c1orf10: cDNA cloning, gene structure,
RT   and frequent loss of expression in esophageal cancer.";
RL   Genomics 69:322-330(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Esophagus;
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 GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
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   INDUCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11606197; DOI=10.1046/j.0014-2956.2001.02468.x;
RA   Yagui-Beltran A., Craig A.L., Lawrie L., Thompson D., Pospisilova S.,
RA   Johnston D., Kernohan N., Hopwood D., Dillon J.F., Hupp T.R.;
RT   "The human oesophageal squamous epithelium exhibits a novel type of heat
RT   shock protein response.";
RL   Eur. J. Biochem. 268:5343-5355(2001).
RN   [7]
RP   SUBUNIT, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15896671; DOI=10.1016/j.biocel.2005.02.005;
RA   Imai F.L., Uzawa K., Nimura Y., Moriya T., Imai M.A., Shiiba M., Bukawa H.,
RA   Yokoe H., Tanzawa H.;
RT   "Chromosome 1 open reading frame 10 (C1orf10) gene is frequently down-
RT   regulated and inhibits cell proliferation in oral squamous cell
RT   carcinoma.";
RL   Int. J. Biochem. Cell Biol. 37:1641-1655(2005).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15854041; DOI=10.1111/j.0022-202x.2005.23694.x;
RA   Contzler R., Favre B., Huber M., Hohl D.;
RT   "Cornulin, a new member of the 'fused gene' family, is expressed during
RT   epidermal differentiation.";
RL   J. Invest. Dermatol. 124:990-997(2005).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=16466100; DOI=10.1177/000348940611500108;
RA   Johnston N., Dettmar P.W., Lively M.O., Postma G.N., Belafsky P.C.,
RA   Birchall M., Koufman J.A.;
RT   "Effect of pepsin on laryngeal stress protein (Sep70, Sep53, and Hsp70)
RT   response: role in laryngopharyngeal reflux disease.";
RL   Ann. Otol. Rhinol. Laryngol. 115:47-58(2006).
RN   [10]
RP   INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16640557; DOI=10.1111/j.1742-4658.2006.05206.x;
RA   Darragh J., Hunter M., Pohler E., Nelson L., Dillon J.F., Nenutil R.,
RA   Vojtesek B., Ross P.E., Kernohan N., Hupp T.R.;
RT   "The calcium-binding domain of the stress protein SEP53 is required for
RT   survival in response to deoxycholic acid-mediated injury.";
RL   FEBS J. 273:1930-1947(2006).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=17289885; DOI=10.1158/1078-0432.ccr-06-1577;
RA   Luthra M.G., Ajani J.A., Izzo J., Ensor J., Wu T.T., Rashid A., Zhang L.,
RA   Phan A., Fukami N., Luthra R.;
RT   "Decreased expression of gene cluster at chromosome 1q21 defines molecular
RT   subgroups of chemoradiotherapy response in esophageal cancers.";
RL   Clin. Cancer Res. 13:912-919(2007).
RN   [12]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND POSSIBLE INVOLVEMENT IN
RP   PSORIASIS.
RX   PubMed=30009832; DOI=10.1016/j.jid.2018.06.184;
RA   Li C., Xiao L., Jia J., Li F., Wang X., Duan Q., Jing H., Yang P., Chen C.,
RA   Wang Q., Liu J., Shao Y., Wang N., Zheng Y.;
RT   "Cornulin Is Induced in Psoriasis Lesions and Promotes Keratinocyte
RT   Proliferation via Phosphoinositide 3-Kinase/Akt Pathways.";
RL   J. Invest. Dermatol. 139:71-80(2019).
RN   [13]
RP   INVOLVEMENT IN ESCR, AND VARIANT ESCR SER-480.
RX   PubMed=19558548; DOI=10.1111/j.1349-7006.2009.01240.x;
RA   Zhang W., Chen X., Luo A., Lin D., Tan W., Liu Z.;
RT   "Genetic variants of C1orf10 and risk of esophageal squamous cell carcinoma
RT   in a Chinese population.";
RL   Cancer Sci. 100:1695-1700(2009).
CC   -!- FUNCTION: Promotes cell proliferation, G1/S cell cycle progression and
CC       induces expression of the cell cycle regulator CCND1 (PubMed:30009832).
CC       Regulates proliferation induced by pro-inflammatory cytokine response
CC       via activation of NFKB1 and PI3K/AKT signaling pathways
CC       (PubMed:30009832). {ECO:0000269|PubMed:30009832}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15896671}.
CC   -!- INTERACTION:
CC       Q9UBG3; P61968: LMO4; NbExp=3; IntAct=EBI-3197866, EBI-2798728;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15854041,
CC       ECO:0000269|PubMed:16640557}. Note=Does not colocalize with TGM1.
CC   -!- TISSUE SPECIFICITY: Expressed in the basal skin layer (at protein
CC       level) (PubMed:30009832). Squamous epithelia cell-specific. Expressed
CC       in the esophagus (periphery of the cells of the granular and the upper
CC       spinous layers), foreskin (granular and lower cornified cells), scalp
CC       skin (granular layer), inner root sheath of the hair follicle and in
CC       primary keratinocytes (at protein level). Expressed in the squamous
CC       epithelium of the cervix, esophagus, foreskin and larynx. Expressed in
CC       the fetal bladder and scalp skin. Expressed at very low levels in the
CC       lung, kidney, uterus, skeletal muscle, heart and fetal brain.
CC       Undetectable or barely detectable in esophageal and oral squamous cell
CC       carcinoma compared with the matched adjacent normal esophageal mucosa.
CC       Undetectable or barely detectable in larynx and esophagus from patients
CC       with pH-documented laryngopharyngeal reflux (LPR).
CC       {ECO:0000269|PubMed:11056050, ECO:0000269|PubMed:11606197,
CC       ECO:0000269|PubMed:15854041, ECO:0000269|PubMed:15896671,
CC       ECO:0000269|PubMed:16466100, ECO:0000269|PubMed:16640557,
CC       ECO:0000269|PubMed:17289885, ECO:0000269|PubMed:30009832}.
CC   -!- INDUCTION: Up-regulated after heat shock, ponasterone A and deoxycholic
CC       acid (PubMed:15896671, PubMed:16640557). Induced in response to pro-
CC       inflammatory cytokines (PubMed:30009832). {ECO:0000269|PubMed:11606197,
CC       ECO:0000269|PubMed:15896671, ECO:0000269|PubMed:16640557,
CC       ECO:0000269|PubMed:30009832}.
CC   -!- DOMAIN: The EF-hand is necessary for the colony survival activity to
CC       protect cells from death induced by exposure to DCA.
CC   -!- DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the
CC       esophagus. The most common types are esophageal squamous cell carcinoma
CC       and adenocarcinoma. Cancer of the esophagus remains a devastating
CC       disease because it is usually not detected until it has progressed to
CC       an advanced incurable stage. {ECO:0000269|PubMed:19558548}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry.
CC   -!- DISEASE: Note=CRNN expression is increased in psoriasis patients
CC       suggesting a potential role in disease pathogenesis.
CC       {ECO:0000269|PubMed:30009832}.
CC   -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
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DR   EMBL; AF077831; AAD55747.1; -; mRNA.
DR   EMBL; AF185276; AAF00514.1; -; Genomic_DNA.
DR   EMBL; AK316568; BAG38157.1; -; mRNA.
DR   EMBL; AL135842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53381.1; -; Genomic_DNA.
DR   EMBL; BC030807; AAH30807.1; -; mRNA.
DR   CCDS; CCDS1010.1; -.
DR   RefSeq; NP_057274.1; NM_016190.2.
DR   AlphaFoldDB; Q9UBG3; -.
DR   SMR; Q9UBG3; -.
DR   BioGRID; 119069; 100.
DR   IntAct; Q9UBG3; 22.
DR   STRING; 9606.ENSP00000271835; -.
DR   iPTMnet; Q9UBG3; -.
DR   PhosphoSitePlus; Q9UBG3; -.
DR   BioMuta; CRNN; -.
DR   DMDM; 74761891; -.
DR   EPD; Q9UBG3; -.
DR   jPOST; Q9UBG3; -.
DR   MassIVE; Q9UBG3; -.
DR   PaxDb; Q9UBG3; -.
DR   PeptideAtlas; Q9UBG3; -.
DR   PRIDE; Q9UBG3; -.
DR   ProteomicsDB; 83965; -.
DR   Antibodypedia; 20343; 149 antibodies from 26 providers.
DR   DNASU; 49860; -.
DR   Ensembl; ENST00000271835.3; ENSP00000271835.3; ENSG00000143536.7.
DR   GeneID; 49860; -.
DR   KEGG; hsa:49860; -.
DR   MANE-Select; ENST00000271835.3; ENSP00000271835.3; NM_016190.3; NP_057274.1.
DR   UCSC; uc001ezx.3; human.
DR   CTD; 49860; -.
DR   DisGeNET; 49860; -.
DR   GeneCards; CRNN; -.
DR   HGNC; HGNC:1230; CRNN.
DR   HPA; ENSG00000143536; Tissue enhanced (esophagus, vagina).
DR   MalaCards; CRNN; -.
DR   MIM; 133239; phenotype.
DR   MIM; 611312; gene.
DR   neXtProt; NX_Q9UBG3; -.
DR   OpenTargets; ENSG00000143536; -.
DR   PharmGKB; PA25601; -.
DR   VEuPathDB; HostDB:ENSG00000143536; -.
DR   eggNOG; ENOG502SATM; Eukaryota.
DR   GeneTree; ENSGT00940000162465; -.
DR   HOGENOM; CLU_043278_0_0_1; -.
DR   InParanoid; Q9UBG3; -.
DR   OMA; TNDQNRG; -.
DR   OrthoDB; 1367189at2759; -.
DR   PhylomeDB; Q9UBG3; -.
DR   TreeFam; TF338665; -.
DR   PathwayCommons; Q9UBG3; -.
DR   SignaLink; Q9UBG3; -.
DR   BioGRID-ORCS; 49860; 7 hits in 1058 CRISPR screens.
DR   GenomeRNAi; 49860; -.
DR   Pharos; Q9UBG3; Tbio.
DR   PRO; PR:Q9UBG3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UBG3; protein.
DR   Bgee; ENSG00000143536; Expressed in lower esophagus mucosa and 91 other tissues.
DR   Genevisible; Q9UBG3; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
DR   GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR   GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR   CDD; cd00213; S-100; 1.
DR   InterPro; IPR026792; Cornulin.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR034325; S-100_dom.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   PANTHER; PTHR11639:SF26; PTHR11639:SF26; 2.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Disease variant; Metal-binding; Reference proteome.
FT   CHAIN           1..495
FT                   /note="Cornulin"
FT                   /id="PRO_0000305586"
FT   DOMAIN          49..84
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          96..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   VARIANT         27
FT                   /note="A -> V (in dbSNP:rs35639220)"
FT                   /id="VAR_048469"
FT   VARIANT         374
FT                   /note="Q -> H (in dbSNP:rs6695830)"
FT                   /id="VAR_048470"
FT   VARIANT         480
FT                   /note="G -> S (in ESCR; dbSNP:rs3829868)"
FT                   /evidence="ECO:0000269|PubMed:19558548"
FT                   /id="VAR_048471"
SQ   SEQUENCE   495 AA;  53533 MW;  C4882A11B4E64DC3 CRC64;
     MPQLLQNING IIEAFRRYAR TEGNCTALTR GELKRLLEQE FADVIVKPHD PATVDEVLRL
     LDEDHTGTVE FKEFLVLVFK VAQACFKTLS ESAEGACGSQ ESGSLHSGAS QELGEGQRSG
     TEVGRAGKGQ HYEGSSHRQS QQGSRGQNRP GVQTQGQATG SAWVSSYDRQ AESQSQERIS
     PQIQLSGQTE QTQKAGEGKR NQTTEMRPER QPQTREQDRA HQTGETVTGS GTQTQAGATQ
     TVEQDSSHQT GRTSKQTQEA TNDQNRGTET HGQGRSQTSQ AVTGGHAQIQ AGTHTQTPTQ
     TVEQDSSHQT GSTSTQTQES TNGQNRGTEI HGQGRSQTSQ AVTGGHTQIQ AGSHTETVEQ
     DRSQTVSHGG AREQGQTQTQ PGSGQRWMQV SNPEAGETVP GGQAQTGAST ESGRQEWSST
     HPRRCVTEGQ GDRQPTVVGE EWVDDHSRET VILRLDQGNL HTSVSSAQGQ DAAQSEEKRG
     ITARELYSYL RSTKP
 
 
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