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CARL3_MOUSE
ID   CARL3_MOUSE             Reviewed;        1375 AA.
AC   Q3UFQ8; Q6KAP3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Capping protein, Arp2/3 and myosin-I linker protein 3 {ECO:0000250|UniProtKB:Q8ND23};
DE   AltName: Full=Capping protein regulator and myosin 1 linker protein 3;
DE   AltName: Full=Leucine-rich repeat-containing protein 16B {ECO:0000312|MGI:MGI:2448573};
GN   Name=Carmil3; Synonyms=Lrrc16b {ECO:0000312|MGI:MGI:2448573};
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].
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT   complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT   by screening of terminal sequences of cDNA clones randomly sampled from
RT   size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-898.
RC   STRAIN=C57BL/6J;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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: Cytoplasm {ECO:0000250|UniProtKB:Q8ND23}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q8ND23}.
CC   -!- DOMAIN: The C-terminus is necessary for localization to the cell
CC       membrane. {ECO:0000250|UniProtKB:Q8ND23}.
CC   -!- SIMILARITY: Belongs to the CARMIL family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21414.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR   EMBL; AK131164; BAD21414.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK148355; BAE28502.1; -; mRNA.
DR   CCDS; CCDS36930.1; -.
DR   RefSeq; NP_001019816.1; NM_001024645.1.
DR   AlphaFoldDB; Q3UFQ8; -.
DR   SMR; Q3UFQ8; -.
DR   BioGRID; 234547; 3.
DR   IntAct; Q3UFQ8; 2.
DR   MINT; Q3UFQ8; -.
DR   STRING; 10090.ENSMUSP00000075587; -.
DR   iPTMnet; Q3UFQ8; -.
DR   PhosphoSitePlus; Q3UFQ8; -.
DR   MaxQB; Q3UFQ8; -.
DR   PaxDb; Q3UFQ8; -.
DR   PRIDE; Q3UFQ8; -.
DR   ProteomicsDB; 265436; -.
DR   Antibodypedia; 22575; 40 antibodies from 12 providers.
DR   DNASU; 268747; -.
DR   Ensembl; ENSMUST00000076236; ENSMUSP00000075587; ENSMUSG00000022211.
DR   GeneID; 268747; -.
DR   KEGG; mmu:268747; -.
DR   UCSC; uc007tyo.1; mouse.
DR   CTD; 90668; -.
DR   MGI; MGI:2448573; Carmil3.
DR   VEuPathDB; HostDB:ENSMUSG00000022211; -.
DR   eggNOG; KOG4242; Eukaryota.
DR   GeneTree; ENSGT00940000157990; -.
DR   HOGENOM; CLU_003119_3_2_1; -.
DR   InParanoid; Q3UFQ8; -.
DR   OMA; NHEHEET; -.
DR   OrthoDB; 208951at2759; -.
DR   PhylomeDB; Q3UFQ8; -.
DR   TreeFam; TF316381; -.
DR   BioGRID-ORCS; 268747; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Lrrc16b; mouse.
DR   PRO; PR:Q3UFQ8; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q3UFQ8; protein.
DR   Bgee; ENSMUSG00000022211; Expressed in embryonic brain and 156 other tissues.
DR   ExpressionAtlas; Q3UFQ8; baseline and differential.
DR   Genevisible; Q3UFQ8; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR029766; CARMIL3.
DR   InterPro; IPR031943; CARMIL_C.
DR   InterPro; IPR041245; CARMIL_PH.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR24112:SF43; PTHR24112:SF43; 1.
DR   Pfam; PF17888; Carm_PH; 1.
DR   Pfam; PF16000; CARMIL_C; 1.
DR   Pfam; PF13516; LRR_6; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Leucine-rich repeat; Membrane;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1375
FT                   /note="Capping protein, Arp2/3 and myosin-I linker protein
FT                   3"
FT                   /id="PRO_0000324609"
FT   REPEAT          244..264
FT                   /note="LRR 1"
FT   REPEAT          274..295
FT                   /note="LRR 2"
FT   REPEAT          303..323
FT                   /note="LRR 3"
FT   REPEAT          335..357
FT                   /note="LRR 4"
FT   REPEAT          365..386
FT                   /note="LRR 5"
FT   REPEAT          392..413
FT                   /note="LRR 6"
FT   REPEAT          424..444
FT                   /note="LRR 7"
FT   REPEAT          455..475
FT                   /note="LRR 8"
FT   REPEAT          482..501
FT                   /note="LRR 9"
FT   REPEAT          509..530
FT                   /note="LRR 10"
FT   REGION          124..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          969..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..897
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..995
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1020
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1074..1099
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1168..1190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1231..1246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1375 AA;  150416 MW;  A6963D11222F14C2 CRC64;
     MAKASVELTR ELQDSIRRCL SQGAVLQQHR VKLETKPKKF EDRVLALTSW RLHLFPLKVP
     AKVESSFNVL EIRAFNTLSQ NQILVETERG TVSMRLPSAE SVDQVTRHVS SALSKVCPGP
     GCLIRRGNAD TPEGPRDTSP NSETSTSTTH SVCGGFSETY AALCDYNGLH CREEVQWDVD
     TIYHAEDNRE FNLLDFSHLE SRDLALMVAA LAYNQWFTKL YCKDLRLGSE VLEQVLHTLS
     KSGSLEELVL DNAGLKTDFV QKLAGVFGEN GSCVLHALIL SHNPIEDKGF LSLSQQLLCF
     PTGLTKLCLA KTAISPRGLQ ALGQTFGANP AFASSLRYLD LSKNPGLLAT DEANALYSFL
     AQPNALVHLD LSGTDCAVDM LLGALLHGCC SHLTYLNLAR NSCSHRKGRE APPAFKQFFS
     SVYTLSHVNL SATRLPLEAL RALLQGLSLN SHLSDLHLDL SSCELRSAGA QALQEQLGAV
     TCIGSLDLSD NGFDSDLLTL VPALGKNKSL KHLFLGKNFN VKAKTLEEIL HKLVQLIQEE
     DCSLQSLSVA DSRLKLRTSI LINALGSNTC LAKVDLSGNG MEDIGAKMLS KALQINSSLR
     TILWDRNNTS ALGFLDIARA LESNHTLRFM SFPVSDISQA YRSAPERTED VWQKIQWCLV
     RNNHSQTCPQ EQAFRLQQGL VTSSAEQMLQ RLCGRVQEEV RALRLCPLEP VQDELLYARD
     LIKDAKNSRA LFPSLYELGH VLANDGPVRQ RLESVASEVS KAVDKELQVI LESMVSLTQE
     LCPVAMRVAE GHNKMLSNVA ERVTVPRNFI RGALLEQAGQ DIQNKLDEVK LSVVTYLTNS
     IVDEILQELY HSHKSLARHL TQLRTLSDPP GGASQGQDPS SRGRGRNHDH EETDDELGTN
     IDTMAIKKQK RCRKIRPVSA FISGSPQDME SQLGSLGIPP GWFSGLGASQ TTASGSWEGL
     SELPTHGYKL RHQTQGRPRP PRTTPPGPGR PSVPVPGPRQ ENGMATRLDE GLEDFFSRRV
     MDESSSYPRT LRTMRPGLSE PPLPPLQKKR RRGLFHFRRP RSFKGDRGPG SPTAGLLLPP
     PPPPPPTQES PPSPDPPSLG NNSSPCWSPE EESSLLPGFG GARGSSFCRK MGTERLEAGE
     GAPAPGTAQQ PRVHGGVALP GLGRTKGWSF DGKREGTDPD QEDSTQAWQK RRSSDDAGPG
     AWKPPPPPQS SKPSFSAMRR AEATWHIAEE SAANHSCQSP SPASQDGDEE KQGALFPERM
     VPTRNAKLQE PPIGPRPPKP VAVPRGRRAP QVPGGREETE SSSAAPGANK PRLRLGSQQD
     QEEPEGQGPT DQGRRTAPLK PKRTRRAQSC DKLEPDRRQP PDPTGVCGTS EPGTD
 
 
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