Full text data of LNP
LNP
(KIAA1715)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Protein lunapark
Protein lunapark
Comments
Isoform Q9C0E8-2 was detected.
Isoform Q9C0E8-2 was detected.
UniProt
Q9C0E8
ID LNP_HUMAN Reviewed; 428 AA.
AC Q9C0E8; Q2M2V8; Q2YD99; Q658W8; Q8N5V9; Q96MS5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-SEP-2006, sequence version 2.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=Protein lunapark;
GN Name=LNP; Synonyms=KIAA1715;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Adrenal cortex, and Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-428.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-194 AND
RP SER-321, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182 AND
RP SER-194, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in limb and central nervous system
CC development (By similarity).
CC -!- INTERACTION:
CC Q9HD42:CHMP1A; NbExp=1; IntAct=EBI-1047206, EBI-1057156;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0E8-2; Sequence=VSP_020239;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9C0E8-3; Sequence=VSP_020238;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the lunapark family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21806.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB051502; BAB21806.1; ALT_INIT; mRNA.
DR EMBL; AK056532; BAB71207.1; -; mRNA.
DR EMBL; BC031530; AAH31530.1; -; mRNA.
DR EMBL; BC105132; AAI05133.1; -; mRNA.
DR EMBL; BC105134; AAI05135.1; -; mRNA.
DR EMBL; BC110329; AAI10330.1; -; mRNA.
DR EMBL; AL832947; CAH56306.1; -; mRNA.
DR RefSeq; NP_085153.1; NM_030650.1.
DR RefSeq; XP_005246934.1; XM_005246877.1.
DR UniGene; Hs.209561; -.
DR ProteinModelPortal; Q9C0E8; -.
DR STRING; 9606.ENSP00000272748; -.
DR PhosphoSite; Q9C0E8; -.
DR DMDM; 114149979; -.
DR PaxDb; Q9C0E8; -.
DR PRIDE; Q9C0E8; -.
DR Ensembl; ENST00000272748; ENSP00000272748; ENSG00000144320.
DR Ensembl; ENST00000409660; ENSP00000386237; ENSG00000144320.
DR GeneID; 80856; -.
DR KEGG; hsa:80856; -.
DR UCSC; uc002ukc.1; human.
DR CTD; 80856; -.
DR GeneCards; GC02M176788; -.
DR HGNC; HGNC:21610; KIAA1715.
DR HPA; HPA014205; -.
DR MIM; 610236; gene.
DR neXtProt; NX_Q9C0E8; -.
DR PharmGKB; PA134938939; -.
DR eggNOG; NOG115207; -.
DR HOGENOM; HOG000231891; -.
DR HOVERGEN; HBG079498; -.
DR InParanoid; Q9C0E8; -.
DR OrthoDB; EOG7ZSHTN; -.
DR GenomeRNAi; 80856; -.
DR NextBio; 71304; -.
DR PMAP-CutDB; Q9C0E8; -.
DR PRO; PR:Q9C0E8; -.
DR ArrayExpress; Q9C0E8; -.
DR Bgee; Q9C0E8; -.
DR CleanEx; HS_KIAA1715; -.
DR Genevestigator; Q9C0E8; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; NAS:UniProtKB.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
DR InterPro; IPR019273; DUF2296.
DR Pfam; PF10058; DUF2296; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Developmental protein; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 428 Protein lunapark.
FT /FTId=PRO_0000248310.
FT TOPO_DOM 2 45 Cytoplasmic (Potential).
FT TRANSMEM 46 66 Helical; (Potential).
FT TOPO_DOM 67 77 Extracellular (Potential).
FT TRANSMEM 78 98 Helical; (Potential).
FT TOPO_DOM 99 428 Cytoplasmic (Potential).
FT COILED 16 41 Potential.
FT COILED 102 128 Potential.
FT COMPBIAS 178 250 Pro-rich.
FT MOD_RES 177 177 Phosphoserine.
FT MOD_RES 182 182 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 321 321 Phosphoserine.
FT MOD_RES 414 414 Phosphoserine (By similarity).
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 1 123 Missing (in isoform 3).
FT /FTId=VSP_020238.
FT VAR_SEQ 1 9 MGGLFSRWR -> MEGK (in isoform 2).
FT /FTId=VSP_020239.
FT CONFLICT 262 262 Y -> H (in Ref. 2; BAB71207).
FT CONFLICT 374 374 E -> G (in Ref. 3; AAH31530).
SQ SEQUENCE 428 AA; 47740 MW; F5BBA4186C2691BF CRC64;
MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS SVLYLFTCLI
VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK RTERNNEALD DLKSQRKKIL
EEVMEKETYK TAKLILERFD PDSKKAKECE PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP
ASPNQGPPPQ VPVSPGPPKD SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP
GPPLARPILP RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN EESLEHDVLD
DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA SVIETNSTVP GADSIPDPEL
SGESLTAE
//
ID LNP_HUMAN Reviewed; 428 AA.
AC Q9C0E8; Q2M2V8; Q2YD99; Q658W8; Q8N5V9; Q96MS5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-SEP-2006, sequence version 2.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=Protein lunapark;
GN Name=LNP; Synonyms=KIAA1715;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Adrenal cortex, and Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-428.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-194 AND
RP SER-321, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182 AND
RP SER-194, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in limb and central nervous system
CC development (By similarity).
CC -!- INTERACTION:
CC Q9HD42:CHMP1A; NbExp=1; IntAct=EBI-1047206, EBI-1057156;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0E8-2; Sequence=VSP_020239;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9C0E8-3; Sequence=VSP_020238;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the lunapark family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21806.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB051502; BAB21806.1; ALT_INIT; mRNA.
DR EMBL; AK056532; BAB71207.1; -; mRNA.
DR EMBL; BC031530; AAH31530.1; -; mRNA.
DR EMBL; BC105132; AAI05133.1; -; mRNA.
DR EMBL; BC105134; AAI05135.1; -; mRNA.
DR EMBL; BC110329; AAI10330.1; -; mRNA.
DR EMBL; AL832947; CAH56306.1; -; mRNA.
DR RefSeq; NP_085153.1; NM_030650.1.
DR RefSeq; XP_005246934.1; XM_005246877.1.
DR UniGene; Hs.209561; -.
DR ProteinModelPortal; Q9C0E8; -.
DR STRING; 9606.ENSP00000272748; -.
DR PhosphoSite; Q9C0E8; -.
DR DMDM; 114149979; -.
DR PaxDb; Q9C0E8; -.
DR PRIDE; Q9C0E8; -.
DR Ensembl; ENST00000272748; ENSP00000272748; ENSG00000144320.
DR Ensembl; ENST00000409660; ENSP00000386237; ENSG00000144320.
DR GeneID; 80856; -.
DR KEGG; hsa:80856; -.
DR UCSC; uc002ukc.1; human.
DR CTD; 80856; -.
DR GeneCards; GC02M176788; -.
DR HGNC; HGNC:21610; KIAA1715.
DR HPA; HPA014205; -.
DR MIM; 610236; gene.
DR neXtProt; NX_Q9C0E8; -.
DR PharmGKB; PA134938939; -.
DR eggNOG; NOG115207; -.
DR HOGENOM; HOG000231891; -.
DR HOVERGEN; HBG079498; -.
DR InParanoid; Q9C0E8; -.
DR OrthoDB; EOG7ZSHTN; -.
DR GenomeRNAi; 80856; -.
DR NextBio; 71304; -.
DR PMAP-CutDB; Q9C0E8; -.
DR PRO; PR:Q9C0E8; -.
DR ArrayExpress; Q9C0E8; -.
DR Bgee; Q9C0E8; -.
DR CleanEx; HS_KIAA1715; -.
DR Genevestigator; Q9C0E8; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; NAS:UniProtKB.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
DR InterPro; IPR019273; DUF2296.
DR Pfam; PF10058; DUF2296; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Developmental protein; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 428 Protein lunapark.
FT /FTId=PRO_0000248310.
FT TOPO_DOM 2 45 Cytoplasmic (Potential).
FT TRANSMEM 46 66 Helical; (Potential).
FT TOPO_DOM 67 77 Extracellular (Potential).
FT TRANSMEM 78 98 Helical; (Potential).
FT TOPO_DOM 99 428 Cytoplasmic (Potential).
FT COILED 16 41 Potential.
FT COILED 102 128 Potential.
FT COMPBIAS 178 250 Pro-rich.
FT MOD_RES 177 177 Phosphoserine.
FT MOD_RES 182 182 Phosphoserine.
FT MOD_RES 194 194 Phosphoserine.
FT MOD_RES 321 321 Phosphoserine.
FT MOD_RES 414 414 Phosphoserine (By similarity).
FT LIPID 2 2 N-myristoyl glycine.
FT VAR_SEQ 1 123 Missing (in isoform 3).
FT /FTId=VSP_020238.
FT VAR_SEQ 1 9 MGGLFSRWR -> MEGK (in isoform 2).
FT /FTId=VSP_020239.
FT CONFLICT 262 262 Y -> H (in Ref. 2; BAB71207).
FT CONFLICT 374 374 E -> G (in Ref. 3; AAH31530).
SQ SEQUENCE 428 AA; 47740 MW; F5BBA4186C2691BF CRC64;
MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS SVLYLFTCLI
VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK RTERNNEALD DLKSQRKKIL
EEVMEKETYK TAKLILERFD PDSKKAKECE PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP
ASPNQGPPPQ VPVSPGPPKD SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP
GPPLARPILP RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY
CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN EESLEHDVLD
DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA SVIETNSTVP GADSIPDPEL
SGESLTAE
//
MIM
610236
*RECORD*
*FIELD* NO
610236
*FIELD* TI
*610236 LUNAPARK
;;LNP;;
KIAA1715
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
read morelibrary, Nagase et al. (2000) cloned KIAA1715. The 3-prime UTR contains
several repetitive elements, and the deduced protein contains 429 amino
acids. RT-PCR ELISA detected high expression in brain, skeletal muscle,
fetal liver, and fetal brain, and intermediate levels in all other
tissues examined. Intermediate to high levels were detected in all
specific adult brain regions examined.
By searching for genes near the HOXD (see HOXD1; 142987) gene cluster in
mouse and human, Spitz et al. (2003) identified a gene they named
Lunapark after the conserved peptide LNPARK in the deduced protein. In
situ hybridization of mouse embryos detected strong staining in limb and
genital buds and weak staining in all other tissues. Expression was
first seen at embryonic day 10.5. Similar staining of developing digits
was seen in embryonic chicken.
GENE STRUCTURE
Spitz et al. (2003) determined that the human and mouse LNP genes
contain 13 exons.
MAPPING
By genomic sequence analysis, Spitz et al. (2003) mapped the LNP gene to
chromosome 2q31. It lies about 80 kb from the 5-prime end of the HOXD
gene cluster and is transcribed from the opposite strand. The mouse Lnp
gene maps to chromosome 2 in a region that shares homology of synteny
with human chromosome 2q31. Spitz et al. (2003) determined that LNP is a
single-copy gene in mammals.
ANIMAL MODEL
The ulnaless (Ul) mutation in mice is a semidominant x-ray-induced
mutation. Heterozygous mice show abnormal zeugopods with an almost
complete absence of ulna. Spitz et al. (2003) determined that Ul is
caused by a balanced paracentric inversion of chromosome 2, with a
centromeric breakpoint into Lnp and a telomeric breakpoint 770 kb away.
The inverted DNA includes Evx2 (142991), the Hoxd complex, Mtx2
(608555), and some pseudogenes. A conserved cluster of global enhancers
is located centromeric to the Lnp breakpoint, and the inversion disrupts
the topographic relationship between the enhancers and their target
genes, thereby altering the expression profile from that chromosomal
segment.
*FIELD* RF
1. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
2. Spitz, F.; Gonzalez, F.; Duboule, D.: A global control region
defines a chromosomal regulatory landscape containing the HoxD cluster. Cell 113:
405-417, 2003.
*FIELD* CD
Patricia A. Hartz: 7/10/2006
*FIELD* ED
wwang: 04/20/2009
mgross: 7/10/2006
*RECORD*
*FIELD* NO
610236
*FIELD* TI
*610236 LUNAPARK
;;LNP;;
KIAA1715
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated adult brain cDNA
read morelibrary, Nagase et al. (2000) cloned KIAA1715. The 3-prime UTR contains
several repetitive elements, and the deduced protein contains 429 amino
acids. RT-PCR ELISA detected high expression in brain, skeletal muscle,
fetal liver, and fetal brain, and intermediate levels in all other
tissues examined. Intermediate to high levels were detected in all
specific adult brain regions examined.
By searching for genes near the HOXD (see HOXD1; 142987) gene cluster in
mouse and human, Spitz et al. (2003) identified a gene they named
Lunapark after the conserved peptide LNPARK in the deduced protein. In
situ hybridization of mouse embryos detected strong staining in limb and
genital buds and weak staining in all other tissues. Expression was
first seen at embryonic day 10.5. Similar staining of developing digits
was seen in embryonic chicken.
GENE STRUCTURE
Spitz et al. (2003) determined that the human and mouse LNP genes
contain 13 exons.
MAPPING
By genomic sequence analysis, Spitz et al. (2003) mapped the LNP gene to
chromosome 2q31. It lies about 80 kb from the 5-prime end of the HOXD
gene cluster and is transcribed from the opposite strand. The mouse Lnp
gene maps to chromosome 2 in a region that shares homology of synteny
with human chromosome 2q31. Spitz et al. (2003) determined that LNP is a
single-copy gene in mammals.
ANIMAL MODEL
The ulnaless (Ul) mutation in mice is a semidominant x-ray-induced
mutation. Heterozygous mice show abnormal zeugopods with an almost
complete absence of ulna. Spitz et al. (2003) determined that Ul is
caused by a balanced paracentric inversion of chromosome 2, with a
centromeric breakpoint into Lnp and a telomeric breakpoint 770 kb away.
The inverted DNA includes Evx2 (142991), the Hoxd complex, Mtx2
(608555), and some pseudogenes. A conserved cluster of global enhancers
is located centromeric to the Lnp breakpoint, and the inversion disrupts
the topographic relationship between the enhancers and their target
genes, thereby altering the expression profile from that chromosomal
segment.
*FIELD* RF
1. Nagase, T.; Kikuno, R.; Hattori, A.; Kondo, Y.; Okumura, K.; Ohara,
O.: Prediction of the coding sequences of unidentified human genes.
XIX. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro. DNA Res. 7: 347-355, 2000.
2. Spitz, F.; Gonzalez, F.; Duboule, D.: A global control region
defines a chromosomal regulatory landscape containing the HoxD cluster. Cell 113:
405-417, 2003.
*FIELD* CD
Patricia A. Hartz: 7/10/2006
*FIELD* ED
wwang: 04/20/2009
mgross: 7/10/2006