SCEL_MOUSE
ID SCEL_MOUSE Reviewed; 652 AA.
AC Q9EQG3; Q9CTT9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sciellin;
GN Name=Scel;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=11112355; DOI=10.1006/geno.2000.6390;
RA Champliaud M.-F., Baden H.P., Koch M., Jin W., Burgeson R.E., Viel A.;
RT "Gene characterization of sciellin (SCEL) and protein localization in
RT vertebrate epithelia displaying barrier properties.";
RL Genomics 70:264-268(2000).
RN [2]
RP SEQUENCE REVISION TO 157; 167-168; 343; 480-481; 508 AND 530-544.
RA Champliaud M.-F., Burgeson R.E., Baden H.P.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-201.
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-343, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May function in the assembly or regulation of proteins in the
CC cornified envelope. The LIM domain may be involved in homotypic or
CC heterotypic associations and may function to localize sciellin to the
CC cornified envelope (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=May become cross-linked
CC to membrane proteins by transglutaminase.
CC -!- TISSUE SPECIFICITY: Expressed in the upper layers of stratified
CC epithelia, including, ependyma and choroid plexus of the brain
CC ventricles.
CC -!- DEVELOPMENTAL STAGE: Strong expression was seen in 17-17.5 day-old
CC embryos. Expression was also detected in the amnion of 17.5 day-old
CC embryo.
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DR EMBL; AF245700; AAG40727.2; -; mRNA.
DR EMBL; AK020346; BAB32078.1; -; mRNA.
DR CCDS; CCDS37002.1; -.
DR RefSeq; NP_075024.2; NM_022886.2.
DR RefSeq; XP_006519418.1; XM_006519355.3.
DR AlphaFoldDB; Q9EQG3; -.
DR IntAct; Q9EQG3; 1.
DR MINT; Q9EQG3; -.
DR STRING; 10090.ENSMUSP00000093233; -.
DR iPTMnet; Q9EQG3; -.
DR PhosphoSitePlus; Q9EQG3; -.
DR MaxQB; Q9EQG3; -.
DR PaxDb; Q9EQG3; -.
DR PRIDE; Q9EQG3; -.
DR ProteomicsDB; 255356; -.
DR Antibodypedia; 24603; 161 antibodies from 26 providers.
DR DNASU; 64929; -.
DR Ensembl; ENSMUST00000095576; ENSMUSP00000093233; ENSMUSG00000022123.
DR GeneID; 64929; -.
DR KEGG; mmu:64929; -.
DR UCSC; uc007uwr.1; mouse.
DR CTD; 8796; -.
DR MGI; MGI:1891228; Scel.
DR VEuPathDB; HostDB:ENSMUSG00000022123; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00530000063872; -.
DR HOGENOM; CLU_399516_0_0_1; -.
DR InParanoid; Q9EQG3; -.
DR OMA; WIYKQTI; -.
DR OrthoDB; 876581at2759; -.
DR PhylomeDB; Q9EQG3; -.
DR TreeFam; TF335114; -.
DR BioGRID-ORCS; 64929; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Scel; mouse.
DR PRO; PR:Q9EQG3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9EQG3; protein.
DR Bgee; ENSMUSG00000022123; Expressed in conjunctival fornix and 115 other tissues.
DR ExpressionAtlas; Q9EQG3; baseline and differential.
DR Genevisible; Q9EQG3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IDA:UniProtKB.
DR GO; GO:0008544; P:epidermis development; IDA:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR InterPro; IPR001781; Znf_LIM.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; LIM domain; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..652
FT /note="Sciellin"
FT /id="PRO_0000075904"
FT REPEAT 207..226
FT /note="1"
FT REPEAT 227..241
FT /note="2"
FT REPEAT 242..261
FT /note="3"
FT REPEAT 262..281
FT /note="4"
FT REPEAT 282..301
FT /note="5"
FT REPEAT 302..320
FT /note="6"
FT REPEAT 321..340
FT /note="7"
FT REPEAT 341..360
FT /note="8"
FT REPEAT 361..380
FT /note="9"
FT REPEAT 381..398
FT /note="10"
FT REPEAT 399..418
FT /note="11"
FT REPEAT 419..438
FT /note="12"
FT REPEAT 439..458
FT /note="13"
FT REPEAT 459..477
FT /note="14"
FT REPEAT 478..496
FT /note="15"
FT DOMAIN 583..649
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..496
FT /note="15 X approximate tandem repeats"
FT REGION 353..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 652 AA; 72972 MW; A089C07DD710EF13 CRC64;
MSNFSSRKKS PTGNDLKSAR GAELRQQGFQ DVNKRRAFLQ DNSWIKKPPE EEQDGNYGRV
VLNRHNSHDA LDRKLIERDE PKATISRYRS EDMLDRTLSS FRTPQSTKTP AVSSFNANTT
ATASTPATTP VKKKRQSWFP PPPPGHNASP STAASRRDPA LHPPLPPKPC SPIASPKPLG
RTNRQIHAAT AGACGETERH AERNIRTEDL DDIIRVAAAL QKTDKGEELD NLIRMNKSLN
RNQGLDGLFR ANLKAQQLDK RAQSLESLIY MNTQTDRDGK GNQAFGSLKK INQRADPDRR
SQDLRSVIRT HATAERIGRR KQDLDGLIKV NPDTNKNMKR GKSLDNLIKV TPEVNRSNKG
GPSLDNFTKG VPARSRANQR DQDLDSLIKV TPSANRSSQH SLDELINTSP QTIKTTARHQ
DLDKFIKVNP DVLTNNQRNH DVDSTIRGNP TGTRCEQSEE LDNLIKVKPS ALRNTNGGQD
LESLTEVNSH VAEKNGRIDG QANGLTNSLF KESTRASVYS YEARNSLSSN SGNKNGGPKD
TVVYTRTYVE NSKSPKDGYQ ENISGKYIQT VYSTSDRSVI ERDMCTYCRK PLGVETKMIL
DELQICCHST CFKCEICKRP LENLQAGDSI WIYRQTIHCE PCYSKVMAKW IQ
