ID D3ZC15_RAT Unreviewed; 1368 AA.
AC D3ZC15;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Capping protein regulator and myosin 1 linker 2 {ECO:0000313|Ensembl:ENSRNOP00000048530.4};
GN Name=Carmil2 {ECO:0000313|Ensembl:ENSRNOP00000048530.4,
GN ECO:0000313|RGD:1562390};
GN Synonyms=RGD1562390 {ECO:0000313|RGD:1562390}, Rltpr
GN {ECO:0000313|RGD:1562390};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000048530.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000048530.4, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000048530.4,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000048530.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000048530.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CARMIL family.
CC {ECO:0000256|ARBA:ARBA00007298}.
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DR RefSeq; XP_008770781.1; XM_008772559.2.
DR RefSeq; XP_008772452.1; XM_008774230.2.
DR AlphaFoldDB; D3ZC15; -.
DR SMR; D3ZC15; -.
DR STRING; 10116.ENSRNOP00000048530; -.
DR PhosphoSitePlus; D3ZC15; -.
DR jPOST; D3ZC15; -.
DR PaxDb; 10116-ENSRNOP00000048530; -.
DR Ensembl; ENSRNOT00000041970.7; ENSRNOP00000048530.4; ENSRNOG00000024452.8.
DR AGR; RGD:1562390; -.
DR RGD; 1562390; Carmil2.
DR eggNOG; KOG4242; Eukaryota.
DR GeneTree; ENSGT00940000161003; -.
DR HOGENOM; CLU_003119_3_1_1; -.
DR InParanoid; D3ZC15; -.
DR OrthoDB; 5476233at2759; -.
DR TreeFam; TF316381; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000024452; Expressed in thymus and 19 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0044354; C:macropinosome; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0051639; P:actin filament network formation; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:RGD.
DR GO; GO:0061339; P:establishment or maintenance of monopolar cell polarity; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:RGD.
DR GO; GO:1902745; P:positive regulation of lamellipodium organization; ISO:RGD.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:RGD.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of type II interferon production; ISO:RGD.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISO:RGD.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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:SF32; CAPPING PROTEIN, ARP2_3 AND MYOSIN-I LINKER PROTEIN 2; 1.
DR PANTHER; PTHR24112; LEUCINE-RICH REPEAT, ISOFORM F-RELATED; 1.
DR Pfam; PF17888; Carm_PH; 1.
DR Pfam; PF16000; CARMIL_C; 1.
DR Pfam; PF13516; LRR_6; 1.
DR SMART; SM00368; LRR_RI; 5.
DR SUPFAM; SSF52047; RNI-like; 1.
PE 1: Evidence at protein level;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 39..119
FT /note="CARMIL pleckstrin homology"
FT /evidence="ECO:0000259|Pfam:PF17888"
FT DOMAIN 780..1071
FT /note="CARMIL C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16000"
FT REGION 923..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..994
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 148360 MW; 3C5B6AE961E99E90 CRC64;
MAHTPDGISC ELRGEITKFL WPKEAELLLK TWLPQEGAEQ SHILALLRWR AYLLHTCLPL
RVDCTFSYLE VQAMALQETP PRVTFELESL PKLVLEFPGV AALEQLAQHV AAAIKKVFPR
STLGKLFRKP TPSSLLARLE KSHPLESTVP SSPCGGFLET YEALCDYNGF PFREEIQWDV
DTIYHRQGCR HFCLGDFSHL GSRDLALSVA ALSYNLWFRR LSCMDMKLSL EVSEQILHMT
SQSSYLEELV LETCGLRGDF VRRLAQALAG HFNSGLRELS LSGNLLDDRG MATLSRHLEH
CPGALRKLCL AQTGLTPRGM RALGRALATN ATFDSTLTHL DLSGNPGALG ASQDGGGLYT
FLSRPNVLAY LNLAGTDTAL GMLFMALSGG CCANLTHLEA SRNIFSRTKS QAVPDALQRF
LGGARMLRHL GLAGCKLPPE ALRALLDGLA LNTQIHDLHL DLSACELRSV GAQVIQDLVC
DAGALSSLDL SDNGFGSDMV TLVLAIGRSR SLKHVALGRN FNVRCKETLD DVLHRIVQLM
QDDDCPLQSL SVAESRLKQG ASVLIRALGT NPKLSVLDIS GNAIGDTGAK MLAKALRVNT
RLRSVIWDRN NTSALGLLDV AEALEQNHSL KSMPLPLNDI TQAHRSRPEL TARAVHQIQA
CLWRNNRADS TSDRKPCLQP LGLISDHSEQ VNELCQSVQE HVELLGCGAG PQGEVAVHQA
EDAIQNANFS LSILPILFEA GSSPSHHWQL QQKLEGLLGQ VGEICRQDIQ DFTQTTLDTT
RSLCPQMLQR PGWRKQLEGV LVGSGGLPEL LPEHLLQDAL TRLRDMRLSI TGTLAENIVA
QALAGLHAAR DRLVESLAQQ APVTVVPAVP PLCGDELTLL ESGGVEEFFF PTEEEEEREK
DDGSSWKWLE PSNCFLVPSL HGAAEEAERD PELAAPGEDA EPQAGPSARG SPSPAAPGPP
AGPLPRMDLP PAGQPLRHPT RARPRPRRQH HHRPPPGGPQ VSPALLQEGN GLTARVDEGV
EEFFSKRLIQ QDRLWAPEED TATEGGTTPV PRTLRKKLGT LFAFKKPRST RGPRPDLETS
PGAAARARKT TLGDLLRPPA RPGRGEEPGG AEGGTSSPDA ARRNRPRYTR ESKAYSMILL
PAEEEAAVGA RPDKRRPLER GDTELAPSFE QRVQVVLQRI GVSRGSGGAE SKRKQSKDGE
IKKAGSDGDI MDSSTETPPI SIKSRTHSVS ADPSCRPGPG GQGPESATWK TLGQQLNAEL
RGRGWGQQDG PGPPSPCPSP SPRRTSPAPD ILSLPEDPCL GPRNEERPLR LQRSPVLKRR
PKLEAPPPPN LGSGLGTKPL PPYPTEPSSP EQSPPSPATD QRGGGPNP
//
