CLMN_MOUSE
ID CLMN_MOUSE Reviewed; 1052 AA.
AC Q8C5W0; Q91V71; Q91XT7; Q91XT8; Q91XU9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Calmin;
DE AltName: Full=Calponin-like transmembrane domain protein;
GN Name=Clmn;
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] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Brain, and Testis;
RX PubMed=11386753; DOI=10.1006/geno.2001.6544;
RA Ishisaki Z., Takaishi M., Furuta I., Huh N.-H.;
RT "Calmin, a protein with calponin homology and transmembrane domains
RT expressed in maturing spermatogenic cells.";
RL Genomics 74:172-179(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-1052 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12670712; DOI=10.1016/s0169-328x(03)00061-5;
RA Takaishi M., Ishisaki Z., Yoshida T., Takata Y., Huh N.-H.;
RT "Expression of calmin, a novel developmentally regulated brain protein with
RT calponin-homology domains.";
RL Brain Res. Mol. Brain Res. 112:146-152(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679 AND SER-925, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Pancreas;
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: [Isoform 1]: Membrane {ECO:0000305}; Single-pass
CC type IV membrane protein {ECO:0000305}. Note=Shows a reticular pattern
CC in the cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Single-pass
CC type IV membrane protein {ECO:0000305}. Note=Shows a reticular pattern
CC in the cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Beta;
CC IsoId=Q8C5W0-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta;
CC IsoId=Q8C5W0-2; Sequence=VSP_007766, VSP_007767;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q8C5W0-3; Sequence=VSP_007768, VSP_007769;
CC Name=4; Synonyms=Alpha;
CC IsoId=Q8C5W0-4; Sequence=VSP_007770;
CC -!- TISSUE SPECIFICITY: Expressed in testis. Expressed during testis
CC maturation process and in maturing spermatids. In brain, it is
CC expressed in neurons of the hippocampus, cerebral cortex, and thalamus,
CC Purkinje cells, and also in the choroid plexus and ependymal cells.
CC Expressed predominantly in dendrites and cell bodies of the neurons,
CC but not in axons. The level of expression increases during the period
CC of maturation of the mouse brain after birth.
CC {ECO:0000269|PubMed:11386753, ECO:0000269|PubMed:12670712}.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks the transmembrane domain.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks the transmembrane domain.
CC {ECO:0000305}.
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DR EMBL; AB047978; BAB59009.1; -; mRNA.
DR EMBL; AB059643; BAB59120.1; -; mRNA.
DR EMBL; AB059644; BAB59121.1; -; mRNA.
DR EMBL; AB059645; BAB59122.1; -; mRNA.
DR EMBL; AB059646; BAB59123.1; -; mRNA.
DR EMBL; AB059647; BAB59124.1; -; mRNA.
DR EMBL; AB059648; BAB59125.1; -; mRNA.
DR EMBL; AK077023; BAC36573.1; -; mRNA.
DR CCDS; CCDS36540.1; -. [Q8C5W0-4]
DR CCDS; CCDS36541.1; -. [Q8C5W0-1]
DR RefSeq; NP_001035772.1; NM_001040682.1. [Q8C5W0-4]
DR RefSeq; NP_444385.2; NM_053155.2. [Q8C5W0-1]
DR AlphaFoldDB; Q8C5W0; -.
DR SMR; Q8C5W0; -.
DR BioGRID; 220420; 5.
DR IntAct; Q8C5W0; 2.
DR MINT; Q8C5W0; -.
DR STRING; 10090.ENSMUSP00000105563; -.
DR iPTMnet; Q8C5W0; -.
DR PhosphoSitePlus; Q8C5W0; -.
DR jPOST; Q8C5W0; -.
DR MaxQB; Q8C5W0; -.
DR PaxDb; Q8C5W0; -.
DR PeptideAtlas; Q8C5W0; -.
DR PRIDE; Q8C5W0; -.
DR ProteomicsDB; 279109; -. [Q8C5W0-1]
DR ProteomicsDB; 279110; -. [Q8C5W0-2]
DR ProteomicsDB; 279111; -. [Q8C5W0-3]
DR ProteomicsDB; 279112; -. [Q8C5W0-4]
DR Antibodypedia; 1167; 52 antibodies from 14 providers.
DR DNASU; 94040; -.
DR Ensembl; ENSMUST00000109936; ENSMUSP00000105562; ENSMUSG00000021097. [Q8C5W0-4]
DR Ensembl; ENSMUST00000109937; ENSMUSP00000105563; ENSMUSG00000021097. [Q8C5W0-1]
DR Ensembl; ENSMUST00000223103; ENSMUSP00000152228; ENSMUSG00000021097. [Q8C5W0-2]
DR Ensembl; ENSMUST00000223177; ENSMUSP00000152097; ENSMUSG00000021097. [Q8C5W0-2]
DR Ensembl; ENSMUST00000223342; ENSMUSP00000152070; ENSMUSG00000021097. [Q8C5W0-2]
DR GeneID; 94040; -.
DR KEGG; mmu:94040; -.
DR UCSC; uc007oxl.1; mouse. [Q8C5W0-1]
DR UCSC; uc011yrj.1; mouse. [Q8C5W0-4]
DR CTD; 79789; -.
DR MGI; MGI:2136957; Clmn.
DR VEuPathDB; HostDB:ENSMUSG00000021097; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000159056; -.
DR HOGENOM; CLU_014038_0_0_1; -.
DR InParanoid; Q8C5W0; -.
DR OMA; PHYEEEG; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; Q8C5W0; -.
DR TreeFam; TF317709; -.
DR BioGRID-ORCS; 94040; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Clmn; mouse.
DR PRO; PR:Q8C5W0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C5W0; protein.
DR Bgee; ENSMUSG00000021097; Expressed in seminiferous tubule of testis and 227 other tissues.
DR ExpressionAtlas; Q8C5W0; baseline and differential.
DR Genevisible; Q8C5W0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR Pfam; PF00307; CH; 2.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1052
FT /note="Calmin"
FT /id="PRO_0000089855"
FT TRANSMEM 1027..1047
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 32..139
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 187..291
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..288
FT /note="Actin-binding"
FT REGION 148..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 710
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96JQ2"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JQ2"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JQ2"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 922..927
FT /note="NSHSDS -> TVIPFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11386753"
FT /id="VSP_007766"
FT VAR_SEQ 928..1052
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11386753"
FT /id="VSP_007767"
FT VAR_SEQ 942..946
FT /note="DHFSY -> SFHLY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11386753"
FT /id="VSP_007768"
FT VAR_SEQ 947..1052
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11386753"
FT /id="VSP_007769"
FT VAR_SEQ 966..996
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11386753"
FT /id="VSP_007770"
FT CONFLICT 170
FT /note="Missing (in Ref. 2; BAC36573)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="S -> R (in Ref. 2; BAC36573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 117227 MW; A5AD7D3FF99A6EB6 CRC64;
MAAQEWDWFQ REELIGQISD IRVQNLQVER ENVQKRTFTR WINLHLEKCD PPLEVTDLFV
DIQDGKILMA LLEVLSGRNL LHEYKSSSHR IFRLNNIAKA LKFLEDSNVK LVSIDAAEIA
DGNPSLVLGL IWNIILFFQI KELTGNLSRS SPSSSLSPGS GGTDSDSSYP PTPTTERSVA
VAVKDQRKAI KTLLSWVQRK TRKYGVAVQD FAGSWRSGLA FLAVIKAIDP SLVDMKQALE
DSTRDNLEKA FSIAHDSLHI PRLLEPEDIM VDMPDEQSIV TYVAQFLERF PELEPEDFVN
PDKEAPIEST FVRIKESPSE QGSRVLLLSE NGERAYTVNQ ETSYPPPDKV FVCDQLESPT
GFCLDSAPSH KLSDSSTEFM HEIIDQVLQG STGKTGSIAE PTPESSILST RKDGRRSNSL
PVKKTVHFEA DLHKDASCSK DPFYSSDFRF EGSPKATKEL SKQDGHVSLA EVSKEKKKSE
QEARLVLEAA SDKVPESTVD GLDAVPQDAQ PSQDSSFCNG TVESPSSQGE KGPPPSSPGD
HTLLANSTEL KVQLLTVEPM DKEDYFECIP LKASKFNRDL VDFASTSQAF GEDPSSHEKT
RGEEEGSENH AEKPGKRKSK SPRAETEAAE SRLEPKKLEP PPKDPEQEDQ GHALPPETPA
DKKPKVYEKA KRKSTRHHSE EEGEAESGFS AVCEEEIPSA PPSTSVSLET LRSHSEEGLD
FKPSPPLSKI SVIPHDLFYY PHYEVPLAAV LEAYAEGGED LKSEDTDLEH PEDSYLQDSR
EEEADEDEEE AQSSQSSCSF SLPVDNSYPS VSEHVSHVDG SSEGPTSALG PGSPPSHEDH
QPKETKENGP VESQQSQEPP NPELPTKPLE EKLTEASTSS KKKEKRKHMD HVESSLFIAP
GTVRSSDDLE ENSSEHKVPS RNSHSDSSIY IRRHTNRSLE LDHFSYVQLR NAADLDDRRN
RVLNRYNSQK LTELILQFYG IRADMKREYK HARLSMTGTN SSGEAVPLGN QSPPNDSLTQ
FVQQPDVIYF ILFLWLLVYC LLLFPQLDVS RL
