CYTSB_MOUSE
ID CYTSB_MOUSE Reviewed; 1067 AA.
AC Q5SXY1; Q5DTQ5; Q5SXY0; Q8BKR3; Q8BL39;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cytospin-B;
DE AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1;
GN Name=Specc1; Synonyms=Cytsb, Kiaa4061;
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 [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-656 (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-847, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-133; SER-136;
RP SER-137; THR-357; SER-360; SER-365; SER-368 AND SER-847, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Membrane
CC {ECO:0000250|UniProtKB:Q5M775}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q5M775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SXY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SXY1-2; Sequence=VSP_021167, VSP_021168;
CC Name=4;
CC IsoId=Q5SXY1-3; Sequence=VSP_021166;
CC -!- SIMILARITY: Belongs to the cytospin-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90492.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220465; BAD90492.1; ALT_INIT; mRNA.
DR EMBL; AL592080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK046469; BAC32744.2; -; mRNA.
DR EMBL; AK050982; BAC34484.2; -; mRNA.
DR AlphaFoldDB; Q5SXY1; -.
DR SMR; Q5SXY1; -.
DR IntAct; Q5SXY1; 2.
DR MINT; Q5SXY1; -.
DR STRING; 10090.ENSMUSP00000090071; -.
DR iPTMnet; Q5SXY1; -.
DR PhosphoSitePlus; Q5SXY1; -.
DR EPD; Q5SXY1; -.
DR jPOST; Q5SXY1; -.
DR MaxQB; Q5SXY1; -.
DR PaxDb; Q5SXY1; -.
DR PeptideAtlas; Q5SXY1; -.
DR PRIDE; Q5SXY1; -.
DR ProteomicsDB; 279141; -. [Q5SXY1-1]
DR ProteomicsDB; 279142; -. [Q5SXY1-2]
DR ProteomicsDB; 279143; -. [Q5SXY1-3]
DR Antibodypedia; 13788; 233 antibodies from 19 providers.
DR Ensembl; ENSMUST00000049836; ENSMUSP00000063102; ENSMUSG00000042331. [Q5SXY1-2]
DR Ensembl; ENSMUST00000092415; ENSMUSP00000090071; ENSMUSG00000042331. [Q5SXY1-3]
DR Ensembl; ENSMUST00000108709; ENSMUSP00000104349; ENSMUSG00000042331. [Q5SXY1-1]
DR Ensembl; ENSMUST00000201624; ENSMUSP00000144659; ENSMUSG00000042331. [Q5SXY1-2]
DR Ensembl; ENSMUST00000201671; ENSMUSP00000144030; ENSMUSG00000042331. [Q5SXY1-2]
DR Ensembl; ENSMUST00000202389; ENSMUSP00000144055; ENSMUSG00000042331. [Q5SXY1-1]
DR Ensembl; ENSMUST00000202905; ENSMUSP00000144311; ENSMUSG00000042331. [Q5SXY1-1]
DR UCSC; uc007jin.2; mouse. [Q5SXY1-3]
DR UCSC; uc033fwe.1; mouse. [Q5SXY1-1]
DR MGI; MGI:2442356; Specc1.
DR VEuPathDB; HostDB:ENSMUSG00000042331; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR InParanoid; Q5SXY1; -.
DR PhylomeDB; Q5SXY1; -.
DR TreeFam; TF316716; -.
DR ChiTaRS; Specc1; mouse.
DR PRO; PR:Q5SXY1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SXY1; protein.
DR Bgee; ENSMUSG00000042331; Expressed in blood and 241 other tissues.
DR ExpressionAtlas; Q5SXY1; baseline and differential.
DR Genevisible; Q5SXY1; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Lipoprotein; Membrane; Myristate;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1067
FT /note="Cytospin-B"
FT /id="PRO_0000254034"
FT DOMAIN 961..1066
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..773
FT /evidence="ECO:0000255"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 77
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M775"
FT VAR_SEQ 1..92
FT /note="MRSAAKPWSPVAKAGSHGPDRTRPLPGTPSGMKSSKSSTSLAFESRLSKLKR
FT ASSEDTLNKPGSASSGVARLKKTSTSGAISELTESRLRSN -> MGNHSAKLEEPE
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_021166"
FT VAR_SEQ 785..790
FT /note="PVNEEP -> SMVSVS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021167"
FT VAR_SEQ 791..1067
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021168"
FT CONFLICT 776..784
FT /note="Missing (in Ref. 1; BAD90492)"
FT /evidence="ECO:0000305"
FT INIT_MET Q5SXY1-3:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q5SXY1-3:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1067 AA; 118101 MW; B199047FB7DF1957 CRC64;
MRSAAKPWSP VAKAGSHGPD RTRPLPGTPS GMKSSKSSTS LAFESRLSKL KRASSEDTLN
KPGSASSGVA RLKKTSTSGA ISELTESRLR SNTGTIPTTK RTGIPAPREL SVTISRERSV
PRGPSSSKKL GSSPTSSCNP TPTKHLRTTP AKPKQEHEGA EKAVLESQVR ELLAEAKTKD
SEINRLRSEL KKCKERWALS TEDANASDPS AEGTASPESD AQPLIRTLEE KNKTFQKELA
DLEEENRALK EKLTYLEQSP NSEGAASHTG DSSCPTSITH ESSFGSPVGN ELSSETDEYR
RTTHGSALRT SGSSSSDVTK ASLSPDASDF EHITADTPSR PLSATSNPFK SSKGSPTGSS
PNNASELSLA SLTEKIQKME ENQHSTAEEL QATLQELSDQ QQMVQELTAE NEKLVDEKTI
LETSFHQHRE RAEQLSQENE KLINLLQERV KNEEPSAQGG KVLELEQKCT DILEKSRFER
EKLLNIQQQL TCSLRKVEEE NQGAIDMIKH LKEENEKLNG FLEHERCNNS VMAKTLEECR
VTLEGLKMEN GSLKALLEAD KQKAIEASST VGQTAENFEV QEMLKVARAE KDQLQLSCTE
LRQELLKANG EIKHVSSLLA KMEKDYSYLK EVCDHQAEQL SRTSLKLQEK ASESDAEIKD
MKETIFELED QVEQHRAVKL HNNQLISELE GSVIKLEEQK SDLERQLKTL TKQIKEETEE
WRRFQADLQT AVVVANDIKC EAQQELRTVK RRLLEEEEKN ARLQKELGDI QGHSRWVTGR
ATLLPVNEEP EPSEADAAGR WRGVYVNRTS PAPSDSATTV KSLIKSFDLG HSGGTGQSIS
VHKTPRSPLS GIPVRTAPAA AVSPMQRHST YSSMKPASKG TSQRLDLPDL PLSDLLKGRA
EDRKSDPYLR KSPSLESLSR PPSLGFGNTR LLSASTGGLK PSKLSVERRD PLAALAREYG
GSKRNALLKW CQKKTEGYAN IDITNFSSSW SDGLALCALL HTYLPAHIPY QELNSQEKKR
NLLLAFEAAQ SVGINPSLEL SEMLYTDRPD WQSVMQYVAQ IYKYFET
