TRPM7_RAT
ID TRPM7_RAT Reviewed; 1862 AA.
AC Q925B3; A7L642;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 7 {ECO:0000312|RGD:620053};
DE EC=2.7.11.1;
DE AltName: Full=Long transient receptor potential channel 7 {ECO:0000250|UniProtKB:Q96QT4};
DE Short=LTrpC-7;
DE Short=LTrpC7 {ECO:0000250|UniProtKB:Q96QT4};
DE AltName: Full=Transient receptor potential-phospholipase C-interacting kinase {ECO:0000303|PubMed:11161216};
DE Short=TRP-PLIK {ECO:0000303|PubMed:11161216};
GN Name=Trpm7 {ECO:0000312|RGD:620053};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK54810.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH PLCB1.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAK54810.1};
RC TISSUE=Brain {ECO:0000269|PubMed:11161216};
RX PubMed=11161216; DOI=10.1126/science.1058519;
RA Runnels L.W., Yue L., Clapham D.E.;
RT "TRP-PLIK, a bifunctional protein with kinase and ion channel activities.";
RL Science 291:1043-1047(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
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 [3] {ECO:0000305, ECO:0000312|EMBL:ABS12242.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 749-866.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ABS12242.1};
RA Sun F.P., Gao T.M.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1198-1248, AND COILED-COIL
RP DOMAIN.
RX PubMed=18782578; DOI=10.1016/j.jmb.2008.08.059;
RA Fujiwara Y., Minor D.L. Jr.;
RT "X-ray crystal structure of a TRPM assembly domain reveals an antiparallel
RT four-stranded coiled-coil.";
RL J. Mol. Biol. 383:854-870(2008).
CC -!- FUNCTION: Essential ion channel and serine/threonine-protein kinase.
CC Divalent cation channel permeable to calcium and magnesium. Has a
CC central role in magnesium ion homeostasis and in the regulation of
CC anoxic neuronal cell death. Involved in TNF-induced necroptosis
CC downstream of MLKL by mediating calcium influx. The kinase activity is
CC essential for the channel function. May be involved in a fundamental
CC process that adjusts plasma membrane divalent cation fluxes according
CC to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1)
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q923J1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q923J1};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q923J1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q923J1};
CC -!- SUBUNIT: Homodimer (By similarity). Forms heterodimers with TRPM6 (By
CC similarity). Interacts with PLCB1. {ECO:0000250,
CC ECO:0000269|PubMed:11161216}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q923J1}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q923J1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305}; Synonyms=TRP-PLIK {ECO:0000269|PubMed:11161216};
CC IsoId=Q925B3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11161216}; Synonyms=PLIK
CC {ECO:0000269|PubMed:11161216};
CC IsoId=Q925B3-2; Sequence=VSP_052983, VSP_052984;
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q923J1}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Alpha-type protein kinase family. ALPK subfamily.
CC {ECO:0000255}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the transient
CC receptor (TC 1.A.4) family. LTrpC subfamily. TRPM7 sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; AF375874; AAK54810.1; -; mRNA.
DR EMBL; AABR03025009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03026190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03028037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03028619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03029036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03029588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03030279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03031904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF673694; ABS12242.1; -; mRNA.
DR PDB; 3E7K; X-ray; 2.01 A; A/B/C/D/E/F/G/H=1198-1249.
DR PDBsum; 3E7K; -.
DR SMR; Q925B3; -.
DR IntAct; Q925B3; 1.
DR MINT; Q925B3; -.
DR STRING; 10116.ENSRNOP00000034169; -.
DR ChEMBL; CHEMBL3721309; -.
DR GuidetoPHARMACOLOGY; 499; -.
DR CarbonylDB; Q925B3; -.
DR iPTMnet; Q925B3; -.
DR PhosphoSitePlus; Q925B3; -.
DR SwissPalm; Q925B3; -.
DR jPOST; Q925B3; -.
DR PaxDb; Q925B3; -.
DR PRIDE; Q925B3; -.
DR ABCD; Q925B3; 1 sequenced antibody.
DR UCSC; RGD:620053; rat. [Q925B3-1]
DR RGD; 620053; Trpm7.
DR eggNOG; KOG3614; Eukaryota.
DR InParanoid; Q925B3; -.
DR PhylomeDB; Q925B3; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR EvolutionaryTrace; Q925B3; -.
DR PRO; PR:Q925B3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0043196; C:varicosity; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IDA:RGD.
DR GO; GO:0005261; F:cation channel activity; IDA:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0016340; P:calcium-dependent cell-matrix adhesion; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; IMP:RGD.
DR GO; GO:0072507; P:divalent inorganic cation homeostasis; IBA:GO_Central.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR Gene3D; 1.20.5.1010; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR InterPro; IPR029601; TRPM7.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF8; PTHR13800:SF8; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Calcium;
KW Calcium channel; Calcium transport; Coiled coil; Ion channel;
KW Ion transport; Kinase; Membrane; Metal-binding; Necrosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; Transport; Zinc.
FT CHAIN 1..1862
FT /note="Transient receptor potential cation channel
FT subfamily M member 7"
FT /id="PRO_0000354664"
FT TOPO_DOM 1..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..962
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1035
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 1036..1056
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1057..1074
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1096..1862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1591..1821
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 544..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1198..1250
FT /evidence="ECO:0000269|PubMed:18782578"
FT COMPBIAS 544..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1764
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1750
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1766
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1774
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1791..1797
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1809
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT BINDING 1813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QT4"
FT MOD_RES 1848
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923J1"
FT VAR_SEQ 1..1515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11161216"
FT /id="VSP_052983"
FT VAR_SEQ 1516..1536
FT /note="PDWLRDRPTNREMPSEGGTLN -> MSELKFILHGCFLKSDLFTIL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11161216"
FT /id="VSP_052984"
FT HELIX 1198..1247
FT /evidence="ECO:0007829|PDB:3E7K"
SQ SEQUENCE 1862 AA; 212376 MW; 25C529CCAA3DC429 CRC64;
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ HACFTASLAT
KYSDVKLGEH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG SHSYRAKYVR LSYDTKPEII
LQLLLKEWQM ELPKLVISVH GGMQKFELHP RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV
AKHVGDALKE HASRSSRKIC TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN
LHSHFILVDD GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI KKTFNFGQSE
AVHLFQTMME CMKKKELITV FHIGSEDHQD IDVAILTALX XGTNASAFDQ LILTLAWDRV
DIAKNHVFVY GQQWLVGSLE QAMLDALVMD RVSFVKLLIE NGVSMHKFLT IPRLEELYNT
KQGPTNPMLF HLIRDVKQGN LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL
GGNNRRSGRN ASSSTPQLRK SHETFGNRAD KKEKMRHNHF IKTAQPYRPK MDASMEEGKK
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA KALVACKIYR
SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ DETMAMKLLT YELKNWSNST
CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR LNMRKNSWYK VILSILVPPA ILMLEYKTKA
EMSHIPQSQD AHQMTMEDSE NNFHNITEEI PMEVFKEVKI LDSSEGKNEM EIHIKSKKLP
ITRKFYAFYH APIVKFWFNT LAYLGFLMLY TFVVLVQMEQ LPSVQEWIVI AYIFTYAIEK
IREVFMSEAG KISQKIKVWF SDYFNVSDTI AIISFFVGFG LRFGAKWNYI NAYDNHVFVA
GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM FYIVVIMALV LLSFGVPRKA
ILYPHEEPSW SLAKDIVFHP YWMIFGEVYA YEIDVCANDS ALPTICGPGT WLTPFLQAVY
LFVQYIIMVN LLIAFFNNVY LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS
LFCCICKRRK KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFDEKDDKFN SGSEERIRVT
FERVEQMSIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT AQKASEASKV
HNEITRELSI SKHLAQNLID DVPVRPMWKK PSVVNTLSSS LPQGDRESNN PFLCNIFMKD
EKDPQYNLFG QDLPVIPQRK EFNIPEAGSS CGALFPSAVS PPELRQRRHG VEMLKIFNKN
QKLGSSPNSS PHMSSPPTKF SVSTPSQPSC KSHLESTTKD PEPIFYKAAE GDNIEFGAFV
GHRDSMDLQR FKETSNKIRE LLSNDTPENT LKHVGAAGYN ECHKTPTSLH SETESCSRRA
STEDSPDVDS RAALLPDWLR DRPTNREMPS EGGTLNGLAS PFKPVLDTNY YYSAVERNNL
MRLSQSIPFV PVPPRGEPVT VYRLEESSPS ILNNSMSSWS QLGLCAKIEF LSKEEMGGGL
RRAVKVLCTW SEHDVLRSGH LYIIKSFLPE VINTWSSIYK EDTVLHLCLR EIQQQRAAQK
LTFAFNQMKP KSIPYSPRFL EVFLLYCHSA GQWFAVEECM TGEFRKYNNN NGDEIIPTNT
LEEIMLAFSH WTYEYTRGEL LVLDLQGVGE NLTDPSVIKA EEKRSCDMVF GPANLGEDAI
KNFRAKHHCN SCCRKLKLPD LKRNDYTPDK IIFPQDESSD LNLQAGNSTK ESEATNSVRL
ML
