PACE1_MOUSE
ID PACE1_MOUSE Reviewed; 735 AA.
AC Q9DBQ7; Q3TRA7; Q6NY01; Q8BQC9; Q8BRJ1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein-associating with the carboxyl-terminal domain of ezrin;
DE AltName: Full=Ezrin-binding protein PACE-1;
DE AltName: Full=SCY1-like protein 3;
GN Name=Scyl3; Synonyms=Pace1;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Embryo, Lung, and Spinal cord;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, 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: May play a role in regulating cell adhesion/migration
CC complexes in migrating cells.
CC -!- SUBUNIT: Interacts with EZR/VIL2 C-terminal domain. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.
CC Note=Colocalized with EZR/VIL2, actin and CD44 in lamellipodia.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DBQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBQ7-2; Sequence=VSP_037985, VSP_013126;
CC Name=3;
CC IsoId=Q9DBQ7-3; Sequence=VSP_027369;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: May be myristoylated; myristoylation may target it to Golgi
CC compartment. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31777.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BC066800; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK004809; BAB23580.1; -; mRNA.
DR EMBL; AK044100; BAC31777.1; ALT_SEQ; mRNA.
DR EMBL; AK050999; BAC34492.1; -; mRNA.
DR EMBL; AK162937; BAE37123.1; -; mRNA.
DR EMBL; BC043085; AAH43085.1; -; mRNA.
DR EMBL; BC066800; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15430.1; -. [Q9DBQ7-1]
DR CCDS; CCDS69967.1; -. [Q9DBQ7-3]
DR RefSeq; NP_001272931.1; NM_001286002.1. [Q9DBQ7-3]
DR RefSeq; NP_001272932.1; NM_001286003.1.
DR RefSeq; NP_083052.1; NM_028776.5. [Q9DBQ7-1]
DR RefSeq; XP_006496912.1; XM_006496849.1.
DR RefSeq; XP_017176061.1; XM_017320572.1.
DR AlphaFoldDB; Q9DBQ7; -.
DR SMR; Q9DBQ7; -.
DR STRING; 10090.ENSMUSP00000027876; -.
DR iPTMnet; Q9DBQ7; -.
DR PhosphoSitePlus; Q9DBQ7; -.
DR EPD; Q9DBQ7; -.
DR MaxQB; Q9DBQ7; -.
DR PaxDb; Q9DBQ7; -.
DR PeptideAtlas; Q9DBQ7; -.
DR PRIDE; Q9DBQ7; -.
DR ProteomicsDB; 294238; -. [Q9DBQ7-1]
DR ProteomicsDB; 294239; -. [Q9DBQ7-2]
DR ProteomicsDB; 294240; -. [Q9DBQ7-3]
DR Antibodypedia; 936; 252 antibodies from 23 providers.
DR DNASU; 240880; -.
DR Ensembl; ENSMUST00000027876; ENSMUSP00000027876; ENSMUSG00000026584. [Q9DBQ7-1]
DR Ensembl; ENSMUST00000161908; ENSMUSP00000125735; ENSMUSG00000026584. [Q9DBQ7-3]
DR Ensembl; ENSMUST00000162234; ENSMUSP00000123704; ENSMUSG00000026584. [Q9DBQ7-2]
DR Ensembl; ENSMUST00000170359; ENSMUSP00000132109; ENSMUSG00000026584. [Q9DBQ7-3]
DR GeneID; 240880; -.
DR KEGG; mmu:240880; -.
DR UCSC; uc007dhq.2; mouse. [Q9DBQ7-1]
DR UCSC; uc011wuu.1; mouse. [Q9DBQ7-3]
DR CTD; 57147; -.
DR MGI; MGI:1921385; Scyl3.
DR VEuPathDB; HostDB:ENSMUSG00000026584; -.
DR eggNOG; KOG1243; Eukaryota.
DR GeneTree; ENSGT00930000151043; -.
DR HOGENOM; CLU_015864_0_0_1; -.
DR InParanoid; Q9DBQ7; -.
DR OMA; PQKNGGI; -.
DR OrthoDB; 1074965at2759; -.
DR PhylomeDB; Q9DBQ7; -.
DR TreeFam; TF313435; -.
DR BioGRID-ORCS; 240880; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Scyl3; mouse.
DR PRO; PR:Q9DBQ7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9DBQ7; protein.
DR Bgee; ENSMUSG00000026584; Expressed in superior cervical ganglion and 228 other tissues.
DR ExpressionAtlas; Q9DBQ7; baseline and differential.
DR Genevisible; Q9DBQ7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0048666; P:neuron development; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Golgi apparatus;
KW Lipoprotein; Myristate; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..735
FT /note="Protein-associating with the carboxyl-terminal
FT domain of ezrin"
FT /id="PRO_0000058168"
FT DOMAIN 2..245
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 194..249
FT /note="HEAT 1"
FT REPEAT 285..323
FT /note="HEAT 2"
FT REPEAT 333..370
FT /note="HEAT 3"
FT REPEAT 372..409
FT /note="HEAT 4"
FT REGION 505..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..735
FT /note="Interaction with EZR"
FT /evidence="ECO:0000250"
FT REGION 604..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZE3"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 56..99
FT /note="HLKTLRHPCLLRFLSCTVEADGIHLVTERVQPLEVALETLSPAE -> MAFT
FT SSLRECSLWKWPWKPCLLQKSVLESMTYCWLLSSFMTEDI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037985"
FT VAR_SEQ 100..735
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013126"
FT VAR_SEQ 319..331
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027369"
FT CONFLICT 93
FT /note="E -> Q (in Ref. 1; BAE37123)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="L -> Q (in Ref. 2; BC066800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 81333 MW; 13E6652AE93A4424 CRC64;
MGSENSALKS YTLRESPFTL PSGLAVYPAI LQDGKCASVF VYKRENEDKV NKAAKHLKTL
RHPCLLRFLS CTVEADGIHL VTERVQPLEV ALETLSPAEV CAGIYDILLA LIFLHDRGHL
THNNVCLSSV FVSEDGHWKL GGMETVCQVP QATPEFLRNI QSVRDPASIP PEEMSPEFSG
LPESHGHARD AYAFGALVDS LLPIFNEQVS ADVLSSFLQI LHSALLNPMP ECRPALSTLL
SHDFFRNDFL EVVNFLKSLT LKSEDEKTEF FKFLLDRVSC LSEELIASRL VPLLLNQLVF
AEPVAVKSFL PYLLGPKKEN APGETPCLLS PALFQSRVIP VLLRLFEVHE EHVRMVLLSH
IEAYVEHFTQ EQLKKVILPQ VLLGLRDTSN SIVAITLRSL AVLVSLLGPE VVVGGERTKI
FKRTAPSFTK TSDLSPEGSP MHVVCSQQSR VSKVLEDPSS NVFPKWLSGN VPSSSRKRIQ
EECYSSLSQT GDQFSHTIKF PMNGLSDVKN TSEDNGSFPA GSNKPEEWPD WSEPEEPEQQ
PASIHRWPRE PCDVAESQHT NLTAEEVTWD DGEASFGTEI NSTATASAPV PVTSGGQSTS
AALVPLTEES KPLQSSPSSK TSHRQHEEVK PPQVSQERPL KAPSGLGLGE EFTIQVKKKP
VQDPELDWFA DMIPEIKPSG TFLILPELRT EVMVPDKDNV SSLMQFSSKF AATEMTEGEA
EGWEGEELAW EDNNW
