Full text data of PLSCR4
PLSCR4
[Confidence: high (present in two of the MS resources)]
Phospholipid scramblase 4; PL scramblase 4 (Ca(2+)-dependent phospholipid scramblase 4; Cell growth-inhibiting gene 43 protein; TRA1)
Phospholipid scramblase 4; PL scramblase 4 (Ca(2+)-dependent phospholipid scramblase 4; Cell growth-inhibiting gene 43 protein; TRA1)
hRBCD
IPI00016776
IPI00016776 Phospholipid scramblase 4 Phospholipid scramblase 4 membrane n/a n/a 1 1 1 1 2 n/a 2 n/a 1 n/a n/a 1 1 n/a 1 1 n/a 1 Type II membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00016776 Phospholipid scramblase 4 Phospholipid scramblase 4 membrane n/a n/a 1 1 1 1 2 n/a 2 n/a 1 n/a n/a 1 1 n/a 1 1 n/a 1 Type II membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q9NRQ2
ID PLS4_HUMAN Reviewed; 329 AA.
AC Q9NRQ2; A8K2E9; Q2TTR3; Q658L3; Q6ZR73; Q7Z505;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Phospholipid scramblase 4;
DE Short=PL scramblase 4;
DE AltName: Full=Ca(2+)-dependent phospholipid scramblase 4;
DE AltName: Full=Cell growth-inhibiting gene 43 protein;
DE AltName: Full=TRA1;
GN Name=PLSCR4; ORFNames=GIG43;
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 [MRNA] (ISOFORM 1), AND VARIANTS SER-34 AND
RP VAL-155.
RC TISSUE=Pancreas;
RX PubMed=10930526; DOI=10.1016/S0005-2736(00)00236-4;
RA Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.;
RT "Identification of three new members of the phospholipid scramblase
RT gene family.";
RL Biochim. Biophys. Acta 1467:244-253(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-34 AND VAL-155.
RA Kim J.W.;
RT "Identification of a human cell growth inhibiting gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thalamus, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-329 (ISOFORM 1).
RA Cui W.C., Yu L., Gao J., Fan Y.X., Xu Y.F., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to murine
RT TRA1 mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.M800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in
RT human phospholipid scramblase 3: differential binding to an
RT alternatively spliced isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [10]
RP COFACTOR, AND MUTAGENESIS OF ASP-290.
RX PubMed=23089641; DOI=10.1515/hsz-2012-0129;
RA Francis V.G., Gummadi S.N.;
RT "Biochemical and functional characterization of human phospholipid
RT scramblase 4 (hPLSCR4).";
RL Biol. Chem. 393:1173-1181(2012).
CC -!- FUNCTION: May mediate accelerated ATP-independent bidirectional
CC transbilayer migration of phospholipids upon binding calcium ions
CC that results in a loss of phospholipid asymmetry in the plasma
CC membrane. May play a central role in the initiation of fibrin clot
CC formation, in the activation of mast cells and in the recognition
CC of apoptotic and injured cells by the reticuloendothelial system.
CC -!- COFACTOR: Calcium or magnesium.
CC -!- SUBUNIT: Interacts with PDCD6.
CC -!- INTERACTION:
CC P09022:Hoxa1 (xeno); NbExp=4; IntAct=EBI-769257, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRQ2-2; Sequence=VSP_042931, VSP_042932;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC liver, kidney, pancreas, spleen, thymus, prostate, testis, uterus,
CC small intestine and colon. Not detected in peripheral blood
CC lymphocytes.
CC -!- SIMILARITY: Belongs to the phospholipid scramblase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97186.1; Type=Frameshift; Positions=152, 155, 163, 325;
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; AF199023; AAF89960.1; -; mRNA.
DR EMBL; AY550971; AAT52217.1; -; mRNA.
DR EMBL; AK128442; BAC87442.1; -; mRNA.
DR EMBL; AK290214; BAF82903.1; -; mRNA.
DR EMBL; AL833760; CAH56232.1; -; mRNA.
DR EMBL; AC092982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78935.1; -; Genomic_DNA.
DR EMBL; BC028354; AAH28354.1; -; mRNA.
DR EMBL; AF087887; AAP97186.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001121776.1; NM_001128304.1.
DR RefSeq; NP_001121777.1; NM_001128305.1.
DR RefSeq; NP_001121778.1; NM_001128306.1.
DR RefSeq; NP_001170775.1; NM_001177304.1.
DR RefSeq; NP_065086.2; NM_020353.2.
DR RefSeq; XP_005247711.1; XM_005247654.1.
DR RefSeq; XP_005247712.1; XM_005247655.1.
DR UniGene; Hs.477869; -.
DR PDB; 3Q5U; X-ray; 2.50 A; B=271-283.
DR PDBsum; 3Q5U; -.
DR ProteinModelPortal; Q9NRQ2; -.
DR IntAct; Q9NRQ2; 16.
DR MINT; MINT-1443866; -.
DR STRING; 9606.ENSP00000347038; -.
DR PhosphoSite; Q9NRQ2; -.
DR DMDM; 212276457; -.
DR PaxDb; Q9NRQ2; -.
DR PRIDE; Q9NRQ2; -.
DR DNASU; 57088; -.
DR Ensembl; ENST00000354952; ENSP00000347038; ENSG00000114698.
DR Ensembl; ENST00000433593; ENSP00000415605; ENSG00000114698.
DR Ensembl; ENST00000446574; ENSP00000399315; ENSG00000114698.
DR Ensembl; ENST00000493382; ENSP00000419040; ENSG00000114698.
DR GeneID; 57088; -.
DR KEGG; hsa:57088; -.
DR UCSC; uc003evt.4; human.
DR CTD; 57088; -.
DR GeneCards; GC03M145910; -.
DR HGNC; HGNC:16497; PLSCR4.
DR HPA; HPA002276; -.
DR MIM; 607612; gene.
DR neXtProt; NX_Q9NRQ2; -.
DR PharmGKB; PA33422; -.
DR eggNOG; NOG317744; -.
DR HOGENOM; HOG000237356; -.
DR HOVERGEN; HBG019157; -.
DR InParanoid; Q9NRQ2; -.
DR OMA; NRYDIKN; -.
DR OrthoDB; EOG77T14X; -.
DR PhylomeDB; Q9NRQ2; -.
DR GeneWiki; PLSCR4; -.
DR GenomeRNAi; 57088; -.
DR NextBio; 62887; -.
DR PRO; PR:Q9NRQ2; -.
DR ArrayExpress; Q9NRQ2; -.
DR Bgee; Q9NRQ2; -.
DR CleanEx; HS_PLSCR4; -.
DR Genevestigator; Q9NRQ2; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; NAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; NAS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR InterPro; IPR005552; Scramblase.
DR PANTHER; PTHR23248; PTHR23248; 1.
DR Pfam; PF03803; Scramblase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Complete proteome;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; SH3-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 329 Phospholipid scramblase 4.
FT /FTId=PRO_0000100792.
FT TOPO_DOM 1 303 Cytoplasmic (By similarity).
FT TRANSMEM 304 320 Helical; (Potential).
FT TOPO_DOM 321 329 Extracellular (By similarity).
FT MOTIF 18 25 SH3-binding 1 (Potential).
FT MOTIF 30 33 WW-binding (Potential).
FT MOTIF 41 49 SH3-binding 2 (Potential).
FT MOTIF 98 106 SH3-binding 3 (Potential).
FT COMPBIAS 195 202 Cys-rich.
FT MOD_RES 83 83 Phosphotyrosine; by ABL (By similarity).
FT MOD_RES 88 88 Phosphotyrosine; by ABL (By similarity).
FT LIPID 250 250 S-palmitoyl cysteine (Probable).
FT LIPID 255 255 S-palmitoyl cysteine (Probable).
FT VAR_SEQ 1 15 Missing (in isoform 2).
FT /FTId=VSP_042931.
FT VAR_SEQ 119 208 Missing (in isoform 2).
FT /FTId=VSP_042932.
FT VARIANT 34 34 N -> S (in dbSNP:rs3762685).
FT /FTId=VAR_011315.
FT VARIANT 155 155 I -> V (in dbSNP:rs1061409).
FT /FTId=VAR_011316.
FT MUTAGEN 290 290 D->A: 50% decrease in scramblase activity
FT in presence of Ca2+, and 40% decrease in
FT scramblase activity in presence of Mg2+.
FT CONFLICT 56 57 LP -> FL (in Ref. 8; AAP97186).
FT CONFLICT 74 74 P -> S (in Ref. 2; AAT52217).
FT CONFLICT 149 149 S -> L (in Ref. 8; AAP97186).
FT CONFLICT 163 163 F -> V (in Ref. 8; AAP97186).
FT CONFLICT 175 175 V -> G (in Ref. 8; AAP97186).
SQ SEQUENCE 329 AA; 37005 MW; 12BE86728D54F794 CRC64;
MSGVVPTAPE QPAGEMENQT KPPDPRPDAP PEYNSHFLPG PPGTAVPPPT GYPGGLPMGY
YSPQQPSTFP LYQPVGGIHP VRYQPGKYPM PNQSVPITWM PGPTPMANCP PGLEYLVQLD
NIHVLQHFEP LEMMTCFETN NRYDIKNNSD QMVYIVTEDT DDFTRNAYRT LRPFVLRVTD
CMGREIMTMQ RPFRCTCCCF CCPSARQELE VQCPPGVTIG FVAEHWNLCR AVYSIQNEKK
ENVMRVRGPC STYGCGSDSV FEVKSLDGIS NIGSIIRKWN GLLSAMADAD HFDIHFPLDL
DVKMKAMIFG ACFLIDFMYF ERSPPQRSR
//
ID PLS4_HUMAN Reviewed; 329 AA.
AC Q9NRQ2; A8K2E9; Q2TTR3; Q658L3; Q6ZR73; Q7Z505;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Phospholipid scramblase 4;
DE Short=PL scramblase 4;
DE AltName: Full=Ca(2+)-dependent phospholipid scramblase 4;
DE AltName: Full=Cell growth-inhibiting gene 43 protein;
DE AltName: Full=TRA1;
GN Name=PLSCR4; ORFNames=GIG43;
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 [MRNA] (ISOFORM 1), AND VARIANTS SER-34 AND
RP VAL-155.
RC TISSUE=Pancreas;
RX PubMed=10930526; DOI=10.1016/S0005-2736(00)00236-4;
RA Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.;
RT "Identification of three new members of the phospholipid scramblase
RT gene family.";
RL Biochim. Biophys. Acta 1467:244-253(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP SER-34 AND VAL-155.
RA Kim J.W.;
RT "Identification of a human cell growth inhibiting gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thalamus, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-329 (ISOFORM 1).
RA Cui W.C., Yu L., Gao J., Fan Y.X., Xu Y.F., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to murine
RT TRA1 mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.M800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in
RT human phospholipid scramblase 3: differential binding to an
RT alternatively spliced isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [10]
RP COFACTOR, AND MUTAGENESIS OF ASP-290.
RX PubMed=23089641; DOI=10.1515/hsz-2012-0129;
RA Francis V.G., Gummadi S.N.;
RT "Biochemical and functional characterization of human phospholipid
RT scramblase 4 (hPLSCR4).";
RL Biol. Chem. 393:1173-1181(2012).
CC -!- FUNCTION: May mediate accelerated ATP-independent bidirectional
CC transbilayer migration of phospholipids upon binding calcium ions
CC that results in a loss of phospholipid asymmetry in the plasma
CC membrane. May play a central role in the initiation of fibrin clot
CC formation, in the activation of mast cells and in the recognition
CC of apoptotic and injured cells by the reticuloendothelial system.
CC -!- COFACTOR: Calcium or magnesium.
CC -!- SUBUNIT: Interacts with PDCD6.
CC -!- INTERACTION:
CC P09022:Hoxa1 (xeno); NbExp=4; IntAct=EBI-769257, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRQ2-2; Sequence=VSP_042931, VSP_042932;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC liver, kidney, pancreas, spleen, thymus, prostate, testis, uterus,
CC small intestine and colon. Not detected in peripheral blood
CC lymphocytes.
CC -!- SIMILARITY: Belongs to the phospholipid scramblase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97186.1; Type=Frameshift; Positions=152, 155, 163, 325;
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; AF199023; AAF89960.1; -; mRNA.
DR EMBL; AY550971; AAT52217.1; -; mRNA.
DR EMBL; AK128442; BAC87442.1; -; mRNA.
DR EMBL; AK290214; BAF82903.1; -; mRNA.
DR EMBL; AL833760; CAH56232.1; -; mRNA.
DR EMBL; AC092982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78935.1; -; Genomic_DNA.
DR EMBL; BC028354; AAH28354.1; -; mRNA.
DR EMBL; AF087887; AAP97186.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001121776.1; NM_001128304.1.
DR RefSeq; NP_001121777.1; NM_001128305.1.
DR RefSeq; NP_001121778.1; NM_001128306.1.
DR RefSeq; NP_001170775.1; NM_001177304.1.
DR RefSeq; NP_065086.2; NM_020353.2.
DR RefSeq; XP_005247711.1; XM_005247654.1.
DR RefSeq; XP_005247712.1; XM_005247655.1.
DR UniGene; Hs.477869; -.
DR PDB; 3Q5U; X-ray; 2.50 A; B=271-283.
DR PDBsum; 3Q5U; -.
DR ProteinModelPortal; Q9NRQ2; -.
DR IntAct; Q9NRQ2; 16.
DR MINT; MINT-1443866; -.
DR STRING; 9606.ENSP00000347038; -.
DR PhosphoSite; Q9NRQ2; -.
DR DMDM; 212276457; -.
DR PaxDb; Q9NRQ2; -.
DR PRIDE; Q9NRQ2; -.
DR DNASU; 57088; -.
DR Ensembl; ENST00000354952; ENSP00000347038; ENSG00000114698.
DR Ensembl; ENST00000433593; ENSP00000415605; ENSG00000114698.
DR Ensembl; ENST00000446574; ENSP00000399315; ENSG00000114698.
DR Ensembl; ENST00000493382; ENSP00000419040; ENSG00000114698.
DR GeneID; 57088; -.
DR KEGG; hsa:57088; -.
DR UCSC; uc003evt.4; human.
DR CTD; 57088; -.
DR GeneCards; GC03M145910; -.
DR HGNC; HGNC:16497; PLSCR4.
DR HPA; HPA002276; -.
DR MIM; 607612; gene.
DR neXtProt; NX_Q9NRQ2; -.
DR PharmGKB; PA33422; -.
DR eggNOG; NOG317744; -.
DR HOGENOM; HOG000237356; -.
DR HOVERGEN; HBG019157; -.
DR InParanoid; Q9NRQ2; -.
DR OMA; NRYDIKN; -.
DR OrthoDB; EOG77T14X; -.
DR PhylomeDB; Q9NRQ2; -.
DR GeneWiki; PLSCR4; -.
DR GenomeRNAi; 57088; -.
DR NextBio; 62887; -.
DR PRO; PR:Q9NRQ2; -.
DR ArrayExpress; Q9NRQ2; -.
DR Bgee; Q9NRQ2; -.
DR CleanEx; HS_PLSCR4; -.
DR Genevestigator; Q9NRQ2; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0017128; F:phospholipid scramblase activity; NAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; NAS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR InterPro; IPR005552; Scramblase.
DR PANTHER; PTHR23248; PTHR23248; 1.
DR Pfam; PF03803; Scramblase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Complete proteome;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; SH3-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 329 Phospholipid scramblase 4.
FT /FTId=PRO_0000100792.
FT TOPO_DOM 1 303 Cytoplasmic (By similarity).
FT TRANSMEM 304 320 Helical; (Potential).
FT TOPO_DOM 321 329 Extracellular (By similarity).
FT MOTIF 18 25 SH3-binding 1 (Potential).
FT MOTIF 30 33 WW-binding (Potential).
FT MOTIF 41 49 SH3-binding 2 (Potential).
FT MOTIF 98 106 SH3-binding 3 (Potential).
FT COMPBIAS 195 202 Cys-rich.
FT MOD_RES 83 83 Phosphotyrosine; by ABL (By similarity).
FT MOD_RES 88 88 Phosphotyrosine; by ABL (By similarity).
FT LIPID 250 250 S-palmitoyl cysteine (Probable).
FT LIPID 255 255 S-palmitoyl cysteine (Probable).
FT VAR_SEQ 1 15 Missing (in isoform 2).
FT /FTId=VSP_042931.
FT VAR_SEQ 119 208 Missing (in isoform 2).
FT /FTId=VSP_042932.
FT VARIANT 34 34 N -> S (in dbSNP:rs3762685).
FT /FTId=VAR_011315.
FT VARIANT 155 155 I -> V (in dbSNP:rs1061409).
FT /FTId=VAR_011316.
FT MUTAGEN 290 290 D->A: 50% decrease in scramblase activity
FT in presence of Ca2+, and 40% decrease in
FT scramblase activity in presence of Mg2+.
FT CONFLICT 56 57 LP -> FL (in Ref. 8; AAP97186).
FT CONFLICT 74 74 P -> S (in Ref. 2; AAT52217).
FT CONFLICT 149 149 S -> L (in Ref. 8; AAP97186).
FT CONFLICT 163 163 F -> V (in Ref. 8; AAP97186).
FT CONFLICT 175 175 V -> G (in Ref. 8; AAP97186).
SQ SEQUENCE 329 AA; 37005 MW; 12BE86728D54F794 CRC64;
MSGVVPTAPE QPAGEMENQT KPPDPRPDAP PEYNSHFLPG PPGTAVPPPT GYPGGLPMGY
YSPQQPSTFP LYQPVGGIHP VRYQPGKYPM PNQSVPITWM PGPTPMANCP PGLEYLVQLD
NIHVLQHFEP LEMMTCFETN NRYDIKNNSD QMVYIVTEDT DDFTRNAYRT LRPFVLRVTD
CMGREIMTMQ RPFRCTCCCF CCPSARQELE VQCPPGVTIG FVAEHWNLCR AVYSIQNEKK
ENVMRVRGPC STYGCGSDSV FEVKSLDGIS NIGSIIRKWN GLLSAMADAD HFDIHFPLDL
DVKMKAMIFG ACFLIDFMYF ERSPPQRSR
//
MIM
607612
*RECORD*
*FIELD* NO
607612
*FIELD* TI
*607612 PHOSPHOLIPID SCRAMBLASE 4; PLSCR4
*FIELD* TX
CLONING
Using the sequence of PLSCR1 (604170) as query, Wiedmer et al. (2000)
read moreidentified an EST containing PLSCR4, and they cloned the full-length
cDNA by PCR of a multiple-tissue cDNA library. The deduced 329-amino
acid protein contains an N-terminal proline-rich region and a C-terminal
Ca(2+)-binding domain. The proline-rich region contains several PxxP
motifs that mediate binding to proteins containing SH3 and WW domains.
PLSCR4 shares 46% identity with PLSCR1, with most of the identity in the
C-terminal region. Northern blot analysis revealed a 4.0-kb transcript
expressed at variable levels in all tissues examined except peripheral
blood lymphocytes. Compared with PLSCR1, PLSCR2 (607610), and PLSCR3
(607611), PLSR4 was the only member of this family expressed at
detectable levels in brain.
MAPPING
By genomic sequence analysis, Wiedmer et al. (2000) mapped the PLSCR4
gene to chromosome 3q23, in a region that also contains the PLSCR1 and
PLSCR2 genes.
*FIELD* RF
1. Wiedmer, T.; Zhou, Q.; Kwoh, D. Y.; Sims, P. J.: Identification
of three new members of the phospholipid scramblase gene family. Biochim.
Biophys. Acta 1467: 244-253, 2000.
*FIELD* CD
Patricia A. Hartz: 3/7/2003
*FIELD* ED
mgross: 03/07/2003
*RECORD*
*FIELD* NO
607612
*FIELD* TI
*607612 PHOSPHOLIPID SCRAMBLASE 4; PLSCR4
*FIELD* TX
CLONING
Using the sequence of PLSCR1 (604170) as query, Wiedmer et al. (2000)
read moreidentified an EST containing PLSCR4, and they cloned the full-length
cDNA by PCR of a multiple-tissue cDNA library. The deduced 329-amino
acid protein contains an N-terminal proline-rich region and a C-terminal
Ca(2+)-binding domain. The proline-rich region contains several PxxP
motifs that mediate binding to proteins containing SH3 and WW domains.
PLSCR4 shares 46% identity with PLSCR1, with most of the identity in the
C-terminal region. Northern blot analysis revealed a 4.0-kb transcript
expressed at variable levels in all tissues examined except peripheral
blood lymphocytes. Compared with PLSCR1, PLSCR2 (607610), and PLSCR3
(607611), PLSR4 was the only member of this family expressed at
detectable levels in brain.
MAPPING
By genomic sequence analysis, Wiedmer et al. (2000) mapped the PLSCR4
gene to chromosome 3q23, in a region that also contains the PLSCR1 and
PLSCR2 genes.
*FIELD* RF
1. Wiedmer, T.; Zhou, Q.; Kwoh, D. Y.; Sims, P. J.: Identification
of three new members of the phospholipid scramblase gene family. Biochim.
Biophys. Acta 1467: 244-253, 2000.
*FIELD* CD
Patricia A. Hartz: 3/7/2003
*FIELD* ED
mgross: 03/07/2003