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K22O_MOUSE
ID   K22O_MOUSE              Reviewed;         594 AA.
AC   Q3UV17;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Keratin, type II cytoskeletal 2 oral {ECO:0000250|UniProtKB:Q01546};
DE   AltName: Full=Keratin-76 {ECO:0000312|MGI:MGI:1924305};
DE            Short=K76;
DE   AltName: Full=Type-II keratin Kb9;
GN   Name=Krt76 {ECO:0000312|MGI:MGI:1924305};
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] {ECO:0000312|EMBL:BAE23456.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23456.1};
RC   TISSUE=Vagina {ECO:0000312|EMBL:BAE23456.1};
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and 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   -!- FUNCTION: Probably contributes to terminal cornification.
CC       {ECO:0000250|UniProtKB:Q01546}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AK137676; BAE23456.1; -; mRNA.
DR   CCDS; CCDS27866.1; -.
DR   RefSeq; NP_001028349.1; NM_001033177.2.
DR   AlphaFoldDB; Q3UV17; -.
DR   SMR; Q3UV17; -.
DR   BioGRID; 218485; 12.
DR   STRING; 10090.ENSMUSP00000097754; -.
DR   iPTMnet; Q3UV17; -.
DR   PhosphoSitePlus; Q3UV17; -.
DR   CPTAC; non-CPTAC-3705; -.
DR   EPD; Q3UV17; -.
DR   jPOST; Q3UV17; -.
DR   MaxQB; Q3UV17; -.
DR   PaxDb; Q3UV17; -.
DR   PeptideAtlas; Q3UV17; -.
DR   PRIDE; Q3UV17; -.
DR   ProteomicsDB; 268941; -.
DR   Antibodypedia; 14669; 511 antibodies from 24 providers.
DR   DNASU; 77055; -.
DR   Ensembl; ENSMUST00000100179; ENSMUSP00000097754; ENSMUSG00000075402.
DR   GeneID; 77055; -.
DR   KEGG; mmu:77055; -.
DR   UCSC; uc007xue.1; mouse.
DR   CTD; 51350; -.
DR   MGI; MGI:1924305; Krt76.
DR   VEuPathDB; HostDB:ENSMUSG00000075402; -.
DR   eggNOG; ENOG502QURK; Eukaryota.
DR   GeneTree; ENSGT00940000162365; -.
DR   HOGENOM; CLU_012560_6_1_1; -.
DR   InParanoid; Q3UV17; -.
DR   OMA; MSHSGMG; -.
DR   OrthoDB; 824246at2759; -.
DR   PhylomeDB; Q3UV17; -.
DR   TreeFam; TF317854; -.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 77055; 4 hits in 71 CRISPR screens.
DR   PRO; PR:Q3UV17; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q3UV17; protein.
DR   Bgee; ENSMUSG00000075402; Expressed in molar tooth and 9 other tissues.
DR   Genevisible; Q3UV17; MM.
DR   GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR   GO; GO:0008544; P:epidermis development; IMP:MGI.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin; Methylation;
KW   Reference proteome.
FT   CHAIN           1..594
FT                   /note="Keratin, type II cytoskeletal 2 oral"
FT                   /id="PRO_0000361693"
FT   DOMAIN          165..480
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..164
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          165..200
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          201..221
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          222..313
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          314..337
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          338..476
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          477..594
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   REGION          497..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         85
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT   MOD_RES         104
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT   MOD_RES         541
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
SQ   SEQUENCE   594 AA;  62845 MW;  00998F2B496DF612 CRC64;
     MSRQACKKSF SCGSQGFSGH SAVVSGSSRS SCVARSGAAS GGACGFRSGA GSLGSHSLYS
     LGGSKSISIS VAAGGSRAGG FSGGRSSCGS GFGSGYGGSL GGSRGMGAGF GGPSGFGGAG
     GFGRPGSFGP GSCPGGIQEV TINQSLLQPL NVEIDPQIGQ VKAQEREQIK TLNNKFASFI
     DKVRFLEQQN KVLETKWELL QQQTIRSGSG PQNLEPFFES YISCLRKQLD SLLGAKGSLE
     GELKSMQDLV EDFKKKYEEE INRRTAAENE FVGLKKDVDG AFMNKVELQA KVDSLTDEIN
     FLRTLYDMEL SQIQSHVSDT SVVLSMDNNR CLDLDSIIAE VKAQYEDIAQ KSKAEAEALY
     QTKLGELQTT AGRHGDDLRS TKSEIMDLNR MIQRLRAEIE NVKKQNTNMQ TSIAEAEQRG
     ERALKDADTK FQDLQVALQK AKEDMARLLK EYQELMNVKL ALDVEIATYR KLLEGEECRL
     SGEFQNAVSI SVVSNVTSTS SSGSFRGTGG SNYGGDSSGR SGGSSSSSSR GSSSRGSSGS
     RLGSGGSISV SQQRMGFNSG GSQTSVGSSY KSGRGGSSSV QFSQTTSSSQ QRSK
 
 
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