KAZRN_MOUSE
ID KAZRN_MOUSE Reviewed; 779 AA.
AC Q69ZS8; A2AC34; B1B0N1; Q8BIY2; Q8R1X4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Kazrin;
GN Name=Kazn; Synonyms=Kaz, Kiaa1026;
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 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary tumor;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=15337775; DOI=10.1083/jcb.200312123;
RA Groot K.R., Sevilla L.M., Nishi K., DiColandrea T., Watt F.M.;
RT "Kazrin, a novel periplakin-interacting protein associated with desmosomes
RT and the keratinocyte plasma membrane.";
RL J. Cell Biol. 166:653-659(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16086310; DOI=10.1002/dvdy.20519;
RA Gallicano G.I., Foshay K., Pengetnze Y., Zhou X.;
RT "Dynamics and unexpected localization of the plakin binding protein,
RT kazrin, in mouse eggs and early embryos.";
RL Dev. Dyn. 234:201-214(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-371, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 -!- FUNCTION: Component of the cornified envelope of keratinocytes. May be
CC involved in the interplay between adherens junctions and desmosomes.
CC The function in the nucleus is not known.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:16086310}.
CC Nucleus {ECO:0000269|PubMed:16086310}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16086310}. Note=In an antibody regognizing isoform
CC 2 and isoform 3 has been used. {ECO:0000269|PubMed:16086310}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q69ZS8-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q69ZS8-2; Sequence=VSP_031905, VSP_031906, VSP_031907;
CC Name=3; Synonyms=C;
CC IsoId=Q69ZS8-3; Sequence=VSP_031904, VSP_031906, VSP_031907;
CC -!- TISSUE SPECIFICITY: Expressed in skin interfollicular epidermis and
CC hair follicles. Expressed in tongue epithelium basal suprabasal layers.
CC {ECO:0000269|PubMed:15337775}.
CC -!- DEVELOPMENTAL STAGE: Expressed in eggs and early embryos. Detected in
CC unfertilized eggs associated with the spindle apparatus and
CC cytoskeletal sheets. As quickly as 5 min after egg activation,
CC relocates to a diffuse peri-spindle position, followed 20-30 min later
CC by localization to the presumptive cytokinetic ring. Before the
CC blastocyst stage of development, associates with the nuclear matrix in
CC a cell cycle-dependent manner, and also associates with the cytoplasmic
CC actin cytoskeleton. After blastocyst formation, is found associating
CC with cell-cell junctions, the cytoskeleton and nucleus.
CC {ECO:0000269|PubMed:16086310}.
CC -!- SIMILARITY: Belongs to the kazrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32368.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173090; BAD32368.1; ALT_INIT; mRNA.
DR EMBL; AK052809; BAC35155.1; -; mRNA.
DR EMBL; AL663037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022941; AAH22941.1; -; mRNA.
DR CCDS; CCDS51350.1; -. [Q69ZS8-2]
DR RefSeq; NP_001103154.1; NM_001109684.1.
DR RefSeq; NP_001103155.1; NM_001109685.1. [Q69ZS8-2]
DR RefSeq; NP_653114.3; NM_144531.3. [Q69ZS8-1]
DR AlphaFoldDB; Q69ZS8; -.
DR SMR; Q69ZS8; -.
DR BioGRID; 214763; 3.
DR STRING; 10090.ENSMUSP00000038835; -.
DR iPTMnet; Q69ZS8; -.
DR PhosphoSitePlus; Q69ZS8; -.
DR MaxQB; Q69ZS8; -.
DR PaxDb; Q69ZS8; -.
DR PRIDE; Q69ZS8; -.
DR ProteomicsDB; 301746; -. [Q69ZS8-1]
DR ProteomicsDB; 301747; -. [Q69ZS8-2]
DR ProteomicsDB; 301748; -. [Q69ZS8-3]
DR Antibodypedia; 28740; 109 antibodies from 19 providers.
DR DNASU; 71529; -.
DR Ensembl; ENSMUST00000036476; ENSMUSP00000038835; ENSMUSG00000040606. [Q69ZS8-2]
DR Ensembl; ENSMUST00000155023; ENSMUSP00000116071; ENSMUSG00000040606. [Q69ZS8-1]
DR GeneID; 71529; -.
DR KEGG; mmu:71529; -.
DR UCSC; uc008vpv.2; mouse. [Q69ZS8-1]
DR UCSC; uc008vpx.2; mouse. [Q69ZS8-2]
DR CTD; 23254; -.
DR MGI; MGI:1918779; Kazn.
DR VEuPathDB; HostDB:ENSMUSG00000040606; -.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT00940000154570; -.
DR InParanoid; Q69ZS8; -.
DR OMA; YKTGRLP; -.
DR PhylomeDB; Q69ZS8; -.
DR TreeFam; TF331216; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 71529; 4 hits in 37 CRISPR screens.
DR ChiTaRS; Kazn; mouse.
DR PRO; PR:Q69ZS8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q69ZS8; protein.
DR Bgee; ENSMUSG00000040606; Expressed in striatum and 66 other tissues.
DR ExpressionAtlas; Q69ZS8; baseline and differential.
DR Genevisible; Q69ZS8; MM.
DR GO; GO:0001533; C:cornified envelope; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030057; C:desmosome; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR CDD; cd09564; SAM_kazrin_repeat1; 1.
DR CDD; cd09567; SAM_kazrin_repeat2; 1.
DR CDD; cd09570; SAM_kazrin_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR037614; Kazrin.
DR InterPro; IPR037613; Kazrin_SAM_rpt_1.
DR InterPro; IPR037615; Kazrin_SAM_rpt_2.
DR InterPro; IPR037616; Kazrin_SAM_rpt_3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12776; PTHR12776; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Keratinization; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..779
FT /note="Kazrin"
FT /id="PRO_0000322454"
FT DOMAIN 450..515
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 528..592
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 616..683
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 295..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 79..261
FT /evidence="ECO:0000255"
FT COMPBIAS 315..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q674X7"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031904"
FT VAR_SEQ 1..80
FT /note="MMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGGPGSGPG
FT AATSASAAAVTVADSAVATMENHQHGAQ -> MRAADSGSWERVRQLAAYGQPTPSCGR
FT DTGSARVPEPGACKLCADTTGLREQQGAGAVPDAADGFGIQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031905"
FT VAR_SEQ 412..425
FT /note="DSDSQCSPTRHSLS -> GTAPDYYIEEDADW (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031906"
FT VAR_SEQ 426..779
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031907"
FT CONFLICT 84
FT /note="R -> Q (in Ref. 1; BAC35155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 86717 MW; 7A8FBD9D840E4126 CRC64;
MMEDNKQLAL RIDGAVQSAS QEVTNLRAEL TATNRRLAEL SGGGGGPGSG PGAATSASAA
AVTVADSAVA TMENHQHGAQ VLLREEVVQL QEEVHLLRQM KEMLAKDLEE SQGGKCSEVL
SATELRVQLV QKEQELARAK EALQAMKADR KRLKGEKTDL VSQMQQLYAT LESREEQLRD
FIRNYEQHRK ESEDAVKALA KEKDLLEREK WELRRQAKEA TDHAAALRSQ LDLKDNRMKE
LEAELAMAKQ SLATLTKDVP KRHSLAMPGE TVLNGNQEWV VQADLPLTAA IRQSQQTLYH
SHPPHPADRQ VRVSPCHSRQ PSVISDASAA EGDRSSTPSD INSPRHRTHS LCNGDSPGPV
QKSLHNPIVQ SLEDLEDQKR KKKKEKMGFG SISRVFARGK QRKSLDPGLF DDSDSQCSPT
RHSLSLSEGE EQMDRLQHVE LVRTTPMSHW KAGTVQAWLE VVMAMPMYVK ACAENVKSGK
VLLSLSDEDL ELGLGVCSSL HRRKLRLAIE DYRDAEAGRS LSKAADLDHH WVAKAWLNDI
GLSQYSQAFQ NHLVDGRMLN SLMKRDLEKH LNVSKKFHQV SILLGIELLY QVNFSREALQ
ERRARCETQN TDPVVWTNQR VLKWVRDIDL KEYADNLTNS GVHGAVLVLE PTFNAEAMAT
ALGIPSGKHI LRRHLAEEMS TIFHPSNSTG IRESERFGTP PGRASSITRA GREDSGGNSK
HRAGRLPLGK IGRGFSSKEP DFHDDYGSLE NEDCGDEDLQ GRPEQCRLEG YGSLEVTNV
