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Protein

F-actin-uncapping protein LRRC16A

Gene

Lrrc16a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028).1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

GO - Biological processi

  • actin filament network formation Source: UniProtKB
  • barbed-end actin filament uncapping Source: UniProtKB
  • cell migration Source: BHF-UCL
  • establishment or maintenance of cell polarity Source: UniProtKB
  • lamellipodium assembly Source: BHF-UCL
  • macropinocytosis Source: UniProtKB
  • negative regulation of barbed-end actin filament capping Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of lamellipodium organization Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • ruffle organization Source: BHF-UCL
  • urate metabolic process Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-uncapping protein LRRC16ABy similarity
Alternative name(s):
CARMIL homologBy similarity
Capping protein, Arp2/3 and myosin-I linker homolog 1By similarity
Capping protein, Arp2/3 and myosin-I linker protein 11 Publication
Short name:
CARML11 Publication
Leucine-rich repeat-containing protein 16AImported
Gene namesi
Name:Lrrc16aImported
Synonyms:CarmilBy similarity, Lrrc16
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1915982. Lrrc16a.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Cell membrane By similarity
  • Cell projectionlamellipodium 1 Publication

  • Note: Found on macropinosomes (By similarity). Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers (PubMed:16054028).By similarity1 Publication

GO - Cellular componenti

  • cell leading edge Source: MGI
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: MGI
  • filamentous actin Source: UniProtKB
  • intermediate filament cytoskeleton Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • macropinosome Source: UniProtKB
  • nucleus Source: BHF-UCL
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi991 – 9911K → A: Decreased ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP. 1 Publication
Mutagenesisi993 – 9931R → A: Loss of ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP. 1 Publication
Mutagenesisi993 – 9931R → E: Loss of ability to bind heterodimeric capping protein (CP) and to inhibit the actin-capping activity of CP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13741374F-actin-uncapping protein LRRC16APRO_0000325816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei122 – 1221PhosphoserineBy similarity
Cross-linki597 – 597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei920 – 9201PhosphothreonineCombined sources
Modified residuei972 – 9721PhosphoserineCombined sources
Modified residuei1096 – 10961PhosphoserineBy similarity
Modified residuei1229 – 12291PhosphothreonineBy similarity
Modified residuei1281 – 12811PhosphoserineBy similarity
Modified residuei1289 – 12891PhosphoserineBy similarity
Modified residuei1291 – 12911PhosphoserineCombined sources
Modified residuei1295 – 12951PhosphoserineCombined sources
Modified residuei1319 – 13191PhosphoserineBy similarity
Modified residuei1328 – 13281PhosphoserineBy similarity
Modified residuei1335 – 13351PhosphoserineCombined sources
Modified residuei1363 – 13631PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6EDY6.
PaxDbiQ6EDY6.
PeptideAtlasiQ6EDY6.
PRIDEiQ6EDY6.

PTM databases

iPTMnetiQ6EDY6.

Expressioni

Gene expression databases

BgeeiQ6EDY6.
CleanExiMM_LRRC16A.
ExpressionAtlasiQ6EDY6. baseline and differential.
GenevisibleiQ6EDY6. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts (via C-terminus) with heterodimeric capping protein (CP); this interaction uncaps barbed ends capped by CP, enhances barbed-end actin polymerization and promotes lamellipodial formation and cell migration (PubMed:16054028). Interacts with MYO1E (By similarity). Interacts with TRIO (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-58942N.
STRINGi10090.ENSMUSP00000072662.

Structurei

Secondary structure

1
1374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 177Combined sources
Beta strandi22 – 243Combined sources
Beta strandi27 – 3610Combined sources
Turni37 – 393Combined sources
Beta strandi40 – 489Combined sources
Beta strandi50 – 6112Combined sources
Beta strandi66 – 694Combined sources
Turni70 – 723Combined sources
Beta strandi73 – 775Combined sources
Beta strandi83 – 908Combined sources
Beta strandi93 – 986Combined sources
Helixi100 – 11617Combined sources
Helixi123 – 1264Combined sources
Beta strandi127 – 1315Combined sources
Helixi135 – 14713Combined sources
Helixi155 – 17016Combined sources
Helixi176 – 18914Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 1994Combined sources
Helixi205 – 2073Combined sources
Helixi208 – 2125Combined sources
Turni213 – 2164Combined sources
Beta strandi222 – 2276Combined sources
Helixi232 – 24413Combined sources
Beta strandi250 – 2545Combined sources
Helixi260 – 27213Combined sources
Beta strandi280 – 2823Combined sources
Helixi291 – 30111Combined sources
Beta strandi308 – 3114Combined sources
Helixi319 – 33113Combined sources
Beta strandi332 – 3343Combined sources
Helixi335 – 3384Combined sources
Beta strandi341 – 3433Combined sources
Beta strandi350 – 3523Combined sources
Helixi355 – 3628Combined sources
Beta strandi369 – 3713Combined sources
Helixi379 – 38911Combined sources
Turni391 – 3933Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi406 – 4083Combined sources
Helixi414 – 4229Combined sources
Beta strandi428 – 4303Combined sources
Helixi438 – 44912Combined sources
Beta strandi456 – 4605Combined sources
Helixi466 – 4727Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi486 – 4927Combined sources
Helixi499 – 5013Combined sources
Helixi502 – 5109Combined sources
Beta strandi517 – 5193Combined sources
Helixi529 – 54416Combined sources
Beta strandi552 – 5543Combined sources
Helixi561 – 5644Combined sources
Helixi565 – 5684Combined sources
Helixi570 – 5734Combined sources
Beta strandi578 – 5814Combined sources
Helixi588 – 60114Combined sources
Beta strandi606 – 6094Combined sources
Helixi617 – 62812Combined sources
Helixi640 – 64910Combined sources
Helixi651 – 66717Combined sources
Beta strandi968 – 9714Combined sources
Helixi989 – 9924Combined sources
Beta strandi1031 – 10344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZ7NMR-C965-1039[»]
3AA0X-ray1.70C985-1005[»]
3AAEX-ray3.30V/W/X/Y/Z971-1002[»]
4K17X-ray2.90A/B/C/D1-668[»]
ProteinModelPortaliQ6EDY6.
SMRiQ6EDY6. Positions 9-668, 965-1039.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6EDY6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati245 – 26925LRR 1Add
BLAST
Repeati275 – 29824LRR 2Add
BLAST
Repeati304 – 32724LRR 3Add
BLAST
Repeati336 – 36328LRR 4Add
BLAST
Repeati391 – 41828LRR 5Add
BLAST
Repeati423 – 44725LRR 6Add
BLAST
Repeati485 – 51026LRR 7Add
BLAST
Repeati547 – 57024LRR 8Add
BLAST
Repeati574 – 59724LRR 9Add
BLAST
Repeati658 – 68225LRR 10Add
BLAST
Repeati962 – 98524LRR 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni962 – 1084123Inhibits capping activity of CP1 PublicationAdd
BLAST
Regioni1058 – 109235Necessary for localization at the cell membraneBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili714 – 73825Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1246 – 12516Poly-Ser
Compositional biasi1253 – 130351Pro-richAdd
BLAST

Domaini

The C-terminus is necessary for localization to the cell membrane.By similarity

Sequence similaritiesi

Belongs to the CARMIL family.Curated
Contains 11 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Coiled coil, Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4242. Eukaryota.
ENOG410Y5JZ. LUCA.
GeneTreeiENSGT00390000014487.
HOGENOMiHOG000230565.
HOVERGENiHBG108094.
InParanoidiQ6EDY6.
OMAiGVDEFFT.
PhylomeDBiQ6EDY6.
TreeFamiTF316381.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR029764. CARMIL1.
IPR031943. CARMIL_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR24112:SF39. PTHR24112:SF39. 1 hit.
PfamiPF16000. CARMIL_C. 1 hit.
PF13516. LRR_6. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6EDY6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTDESSDVPR ELMESIKDVI GRKIKISVKK KVKLEVKGDR VENKVLVLTS
60 70 80 90 100
CRAFLLSARI PSKLELTFSY LEIHGVICHK PAQMVVETEK CNMSMKMVSP
110 120 130 140 150
EDVSEVLAHI GTCLRRIFPG LSPLRIMKKV SMEPSERLAS LQALWDSQTL
160 170 180 190 200
AEPGPCGGFS QMYACVCDWL GFSYKEEVQW DVDTIYLTQD TRELNLQDFS
210 220 230 240 250
HLEHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR VVSRSNRLEE
260 270 280 290 300
LVLENAGLRI DFAQKLAGAL AHNPNSGLHT INLAGNSLED RGVSSLSIQF
310 320 330 340 350
AKLPKGLKHL NLSKTSLSPK GVNSLCQSLS ANPLTASTLT HLDLSGNALR
360 370 380 390 400
GDDLSHMYNF LAQPNTIVHL DLSNTECSLE MVCSALLRGC LQCLAVLNLS
410 420 430 440 450
RSVFSHRKGK EVPPSFKQFF SSSLALIQIN LSGTKLSPEP LKALLLGLAC
460 470 480 490 500
NHSLKGVSLD LSNCELGHCL RSGGAQVLEG CIAEIHNITS LDISDNGLES
510 520 530 540 550
DLSTLIVWLS KNRSIQHLAL GKNFNNMKSK NLTPVLDNLV QMIQDEDSPL
560 570 580 590 600
QSLSLADSKL KAEVTIIINA LGSNTSLTKV DISGNGMGDM GAKMLAKALQ
610 620 630 640 650
INTKLRTVIW DKNNITAQGF QDIAVAMEKN YTLRFMPIPM YDAAQALKTN
660 670 680 690 700
PEKTEEALQK IENYLLRNHE TRKYLQEQAY RLQQGIVTST TQQMIDRICV
710 720 730 740 750
KVQDHLNSLR ACGGDAIQED LKAAERLMRD AKNSKTLLPN LYHVGGASWA
760 770 780 790 800
GASGLSSSPI QETLESMAGE VTRVVDEQLK DLLESMVDAA ETLCPNVMRK
810 820 830 840 850
AHIRQDLIHA STEKISIPRT FVKNVLLEQS GIDILNKISE VKLTVASFLS
860 870 880 890 900
DRIVDEILDS LSSSHRKLAN HFSRLNKSLP QREDLEVELV EEKPVKRAIL
910 920 930 940 950
TVEDLTEVER LEDLDTCMMT PKSKRKSIHS RMLRPVSRAF EMEFDLDKAL
960 970 980 990 1000
EEVPIHIEDP PFPSVRQEKR SSGLISELPS EEGRRLEHFT KLRPKRNKKQ
1010 1020 1030 1040 1050
QPTQAAVCTI SILPQDGEQN GLMGRVDEGV DEFFTKKVTK MDCKRSSSRS
1060 1070 1080 1090 1100
SDAHELGEGD EKKKRDSRRS GFLNLIKSRS RSERPPTVLM TEELSSPKGA
1110 1120 1130 1140 1150
MRSPPVDTTR KEIKAAEHNG APDRTEEIKT PEPLEEGPAE EAGRAERSDS
1160 1170 1180 1190 1200
RGSPQGGRRY VQVMGSGLLA EMKAKQERRA ACAQKKLGND VISQDPSSPV
1210 1220 1230 1240 1250
SCNTERLEGG ATVPKLQPGL PEARFGSGTP EKNAKAEPRV DGGCRSRSSS
1260 1270 1280 1290 1300
SMPTSPKPLL QSPKPSPSAR PSIPQKPRTA SRPEDTPDSP SGPSSPKVAL
1310 1320 1330 1340 1350
LPPILKKVSS DKERDGQNSS QSSPRSFSQE ASRRSWGPAQ EYQEQKQRSS
1360 1370
GKDGHQGSKC SDSGEEAEKE FIFV
Length:1,374
Mass (Da):151,860
Last modified:March 18, 2008 - v2
Checksum:iA7BE0350B3770101
GO
Isoform 2 (identifier: Q6EDY6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     260-260: I → M
     261-1374: Missing.

Note: No experimental confirmation available.
Show »
Length:260
Mass (Da):29,654
Checksum:i280BFD09C54C5F28
GO
Isoform 3 (identifier: Q6EDY6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     918-918: M → MTLCCTS
     1332-1374: SRRSWGPAQEYQEQKQRSSGKDGHQGSKCSDSGEEAEKEFIFV → CPTNF

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:1,342
Mass (Da):148,175
Checksum:iD89ED3FEEE6C9136
GO

Sequence cautioni

The sequence AAH12229.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC31591.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81V → A in AAR96060 (PubMed:16054028).Curated
Sequence conflicti782 – 7821L → W in AAR96060 (PubMed:16054028).Curated
Sequence conflicti782 – 7821L → W in AAH12229 (PubMed:15489334).Curated
Sequence conflicti796 – 7961N → S in AAH12229 (PubMed:15489334).Curated
Sequence conflicti1309 – 13091S → P in AAR96060 (PubMed:16054028).Curated
Sequence conflicti1309 – 13091S → P in AAH12229 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei260 – 2601I → M in isoform 2. 1 PublicationVSP_032421
Alternative sequencei261 – 13741114Missing in isoform 2. 1 PublicationVSP_032422Add
BLAST
Alternative sequencei918 – 9181M → MTLCCTS in isoform 3. 1 PublicationVSP_032423
Alternative sequencei1332 – 137443SRRSW…EFIFV → CPTNF in isoform 3. 1 PublicationVSP_032424Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY437876 mRNA. Translation: AAR96060.1.
AK051570 mRNA. Translation: BAC34678.1.
AK043591 mRNA. Translation: BAC31591.1. Different initiation.
AL606464, AL590864, AL683873 Genomic DNA. Translation: CAI35972.2.
BC012229 mRNA. Translation: AAH12229.1. Different initiation.
CCDSiCCDS36621.1. [Q6EDY6-1]
RefSeqiNP_081101.3. NM_026825.3. [Q6EDY6-1]
XP_011242640.1. XM_011244338.1. [Q6EDY6-3]
XP_011242641.1. XM_011244339.1. [Q6EDY6-3]
UniGeneiMm.211047.

Genome annotation databases

EnsembliENSMUST00000072889; ENSMUSP00000072662; ENSMUSG00000021338. [Q6EDY6-1]
GeneIDi68732.
KEGGimmu:68732.
UCSCiuc007pvn.1. mouse. [Q6EDY6-1]
uc007pvp.1. mouse. [Q6EDY6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY437876 mRNA. Translation: AAR96060.1.
AK051570 mRNA. Translation: BAC34678.1.
AK043591 mRNA. Translation: BAC31591.1. Different initiation.
AL606464, AL590864, AL683873 Genomic DNA. Translation: CAI35972.2.
BC012229 mRNA. Translation: AAH12229.1. Different initiation.
CCDSiCCDS36621.1. [Q6EDY6-1]
RefSeqiNP_081101.3. NM_026825.3. [Q6EDY6-1]
XP_011242640.1. XM_011244338.1. [Q6EDY6-3]
XP_011242641.1. XM_011244339.1. [Q6EDY6-3]
UniGeneiMm.211047.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZ7NMR-C965-1039[»]
3AA0X-ray1.70C985-1005[»]
3AAEX-ray3.30V/W/X/Y/Z971-1002[»]
4K17X-ray2.90A/B/C/D1-668[»]
ProteinModelPortaliQ6EDY6.
SMRiQ6EDY6. Positions 9-668, 965-1039.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58942N.
STRINGi10090.ENSMUSP00000072662.

PTM databases

iPTMnetiQ6EDY6.

Proteomic databases

MaxQBiQ6EDY6.
PaxDbiQ6EDY6.
PeptideAtlasiQ6EDY6.
PRIDEiQ6EDY6.

Protocols and materials databases

DNASUi68732.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072889; ENSMUSP00000072662; ENSMUSG00000021338. [Q6EDY6-1]
GeneIDi68732.
KEGGimmu:68732.
UCSCiuc007pvn.1. mouse. [Q6EDY6-1]
uc007pvp.1. mouse. [Q6EDY6-2]

Organism-specific databases

CTDi55604.
MGIiMGI:1915982. Lrrc16a.

Phylogenomic databases

eggNOGiKOG4242. Eukaryota.
ENOG410Y5JZ. LUCA.
GeneTreeiENSGT00390000014487.
HOGENOMiHOG000230565.
HOVERGENiHBG108094.
InParanoidiQ6EDY6.
OMAiGVDEFFT.
PhylomeDBiQ6EDY6.
TreeFamiTF316381.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiLrrc16a. mouse.
EvolutionaryTraceiQ6EDY6.
PROiQ6EDY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ6EDY6.
CleanExiMM_LRRC16A.
ExpressionAtlasiQ6EDY6. baseline and differential.
GenevisibleiQ6EDY6. MM.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR029764. CARMIL1.
IPR031943. CARMIL_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR24112:SF39. PTHR24112:SF39. 1 hit.
PfamiPF16000. CARMIL_C. 1 hit.
PF13516. LRR_6. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian CARMIL inhibits actin filament capping by capping protein."
    Yang C., Pring M., Wear M.A., Huang M., Cooper J.A., Svitkina T.M., Zigmond S.H.
    Dev. Cell 9:209-221(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN-CAPPING PROTEIN, MUTAGENESIS OF LYS-991 AND ARG-993.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1374 (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Brain cortex and Spinal ganglion.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-1374 (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-920; SER-972; SER-1291; SER-1295; SER-1335 AND SER-1363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCARL1_MOUSE
AccessioniPrimary (citable) accession number: Q6EDY6
Secondary accession number(s): Q5NCM0
, Q8BQ45, Q8BRS5, Q91YZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 6, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.