LMTK1_HUMAN
ID LMTK1_HUMAN Reviewed; 1374 AA.
AC Q6ZMQ8; O75136; Q6ZN31; Q86X28;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Serine/threonine-protein kinase LMTK1;
DE EC=2.7.11.1;
DE AltName: Full=Apoptosis-associated tyrosine kinase;
DE Short=AATYK;
DE AltName: Full=Brain apoptosis-associated tyrosine kinase;
DE AltName: Full=CDK5-binding protein;
DE AltName: Full=Lemur tyrosine kinase 1;
DE AltName: Full=p35-binding protein;
DE Short=p35BP;
GN Name=AATK; Synonyms=AATYK, KIAA0641, LMR1, LMTK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP CYS-703.
RC TISSUE=Cerebellum, and Thalamus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-1374 (ISOFORM 1), AND VARIANT
RP CYS-703.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 786-1374 (ISOFORM 1), AND VARIANT
RP SER-1266.
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORM 2), INTERACTION WITH CDK5, AND
RP PHOSPHORYLATION.
RX PubMed=14521924; DOI=10.1016/j.bbrc.2003.08.143;
RA Honma N., Asada A., Takeshita S., Enomoto M., Yamakawa E., Tsutsumi K.,
RA Saito T., Satoh T., Itoh H., Kaziro Y., Kishimoto T., Hisanaga S.;
RT "Apoptosis-associated tyrosine kinase is a Cdk5 activator p35 binding
RT protein.";
RL Biochem. Biophys. Res. Commun. 310:398-404(2003).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10837911; DOI=10.1016/s0169-328x(00)00048-6;
RA Raghunath M., Patti R., Bannerman P., Lee C.M., Baker S., Sutton L.N.,
RA Phillips P.C., Damodar Reddy C.;
RT "A novel kinase, AATYK induces and promotes neuronal differentiation in a
RT human neuroblastoma (SH-SY5Y) cell line.";
RL Brain Res. Mol. Brain Res. 77:151-162(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-1262, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP VARIANTS PHE-81; VAL-97; VAL-104; CYS-703; ARG-815; LEU-923; LYS-1160;
RP SER-1192; SER-1266 AND THR-1332.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: May be involved in neuronal differentiation.
CC {ECO:0000269|PubMed:10837911}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with CDK5. {ECO:0000269|PubMed:14521924}.
CC -!- INTERACTION:
CC Q6ZMQ8; P62136: PPP1CA; NbExp=3; IntAct=EBI-2008380, EBI-357253;
CC Q6ZMQ8; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-2008380, EBI-11139477;
CC Q6ZMQ8-1; Q15078: CDK5R1; NbExp=2; IntAct=EBI-2008436, EBI-746189;
CC Q6ZMQ8-2; Q15078: CDK5R1; NbExp=6; IntAct=EBI-2008441, EBI-746189;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:10837911}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10837911}. Note=Predominantly perinuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZMQ8-1; Sequence=Displayed;
CC Name=2; Synonyms=hAATYKs-p35BP;
CC IsoId=Q6ZMQ8-2; Sequence=VSP_020225, VSP_020226, VSP_020227,
CC VSP_020228;
CC Name=3;
CC IsoId=Q6ZMQ8-3; Sequence=VSP_020226, VSP_020227, VSP_020228;
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:10837911}.
CC -!- INDUCTION: Up-regulated during apoptosis.
CC -!- PTM: Autophosphorylated. Phosphorylated by CDK5.
CC {ECO:0000269|PubMed:14521924}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AK131395; BAD18544.1; -; mRNA.
DR EMBL; AK131529; BAD18667.1; -; mRNA.
DR EMBL; AB014541; BAA31616.2; -; mRNA.
DR EMBL; BC047378; AAH47378.1; -; mRNA.
DR CCDS; CCDS45807.1; -. [Q6ZMQ8-1]
DR RefSeq; NP_001073864.2; NM_001080395.2. [Q6ZMQ8-1]
DR RefSeq; NP_004911.2; NM_004920.2.
DR AlphaFoldDB; Q6ZMQ8; -.
DR SMR; Q6ZMQ8; -.
DR BioGRID; 114984; 60.
DR IntAct; Q6ZMQ8; 60.
DR MINT; Q6ZMQ8; -.
DR STRING; 9606.ENSP00000324196; -.
DR TCDB; 8.A.23.1.35; the basigin (basigin) family.
DR iPTMnet; Q6ZMQ8; -.
DR PhosphoSitePlus; Q6ZMQ8; -.
DR BioMuta; AATK; -.
DR DMDM; 114149222; -.
DR jPOST; Q6ZMQ8; -.
DR MassIVE; Q6ZMQ8; -.
DR MaxQB; Q6ZMQ8; -.
DR PaxDb; Q6ZMQ8; -.
DR PeptideAtlas; Q6ZMQ8; -.
DR PRIDE; Q6ZMQ8; -.
DR ProteomicsDB; 67901; -. [Q6ZMQ8-1]
DR ProteomicsDB; 67902; -. [Q6ZMQ8-2]
DR ProteomicsDB; 67903; -. [Q6ZMQ8-3]
DR Antibodypedia; 2104; 213 antibodies from 28 providers.
DR DNASU; 9625; -.
DR Ensembl; ENST00000326724.9; ENSP00000324196.4; ENSG00000181409.14. [Q6ZMQ8-1]
DR Ensembl; ENST00000374792.6; ENSP00000363924.2; ENSG00000181409.14. [Q6ZMQ8-3]
DR GeneID; 9625; -.
DR KEGG; hsa:9625; -.
DR MANE-Select; ENST00000326724.9; ENSP00000324196.4; NM_001080395.3; NP_001073864.2.
DR UCSC; uc010dia.4; human. [Q6ZMQ8-1]
DR CTD; 9625; -.
DR DisGeNET; 9625; -.
DR GeneCards; AATK; -.
DR HGNC; HGNC:21; AATK.
DR HPA; ENSG00000181409; Tissue enriched (brain).
DR MIM; 605276; gene.
DR neXtProt; NX_Q6ZMQ8; -.
DR OpenTargets; ENSG00000181409; -.
DR PharmGKB; PA24370; -.
DR VEuPathDB; HostDB:ENSG00000181409; -.
DR eggNOG; ENOG502RCHK; Eukaryota.
DR GeneTree; ENSGT00940000154244; -.
DR HOGENOM; CLU_004618_1_0_1; -.
DR InParanoid; Q6ZMQ8; -.
DR OMA; MACEVSC; -.
DR OrthoDB; 53680at2759; -.
DR PhylomeDB; Q6ZMQ8; -.
DR TreeFam; TF332280; -.
DR PathwayCommons; Q6ZMQ8; -.
DR SignaLink; Q6ZMQ8; -.
DR SIGNOR; Q6ZMQ8; -.
DR BioGRID-ORCS; 9625; 21 hits in 1104 CRISPR screens.
DR GeneWiki; AATK; -.
DR GenomeRNAi; 9625; -.
DR Pharos; Q6ZMQ8; Tbio.
DR PRO; PR:Q6ZMQ8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6ZMQ8; protein.
DR Bgee; ENSG00000181409; Expressed in sural nerve and 181 other tissues.
DR ExpressionAtlas; Q6ZMQ8; baseline and differential.
DR Genevisible; Q6ZMQ8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd05087; PTKc_Aatyk1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042817; LMTK1_c.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1374
FT /note="Serine/threonine-protein kinase LMTK1"
FT /id="PRO_0000248300"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 125..395
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 542..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1090
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 131..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YE4"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YE4"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YE4"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YE4"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YE4"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..433
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020225"
FT VAR_SEQ 468..503
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020226"
FT VAR_SEQ 897..915
FT /note="VGTPDSLDSLDIPSSASDG -> WPQREESLPRLCLLLRPRG (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020227"
FT VAR_SEQ 916..1374
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020228"
FT VARIANT 81
FT /note="S -> F (in an ovarian mucinous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032679"
FT VARIANT 97
FT /note="L -> V (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032680"
FT VARIANT 104
FT /note="M -> V (in an ovarian mucinous carcinoma sample;
FT somatic mutation; dbSNP:rs1337040042)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032681"
FT VARIANT 118
FT /note="T -> M (in dbSNP:rs8082016)"
FT /id="VAR_027267"
FT VARIANT 703
FT /note="G -> C (in dbSNP:rs7503604)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:9734811"
FT /id="VAR_032682"
FT VARIANT 815
FT /note="S -> R (in dbSNP:rs56032966)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032683"
FT VARIANT 923
FT /note="S -> L (in dbSNP:rs56313973)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032684"
FT VARIANT 1160
FT /note="E -> K (in dbSNP:rs55793641)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032685"
FT VARIANT 1192
FT /note="P -> S (in dbSNP:rs55856613)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032686"
FT VARIANT 1266
FT /note="F -> S (in dbSNP:rs36000545)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_032687"
FT VARIANT 1332
FT /note="A -> T (in dbSNP:rs55713566)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_032688"
FT CONFLICT 49..63
FT /note="MLACLCCKKGGIGFK -> HQVKVQGCWGRWRWQ (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="A -> T (in Ref. 1; BAD18667)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="A -> T (in Ref. 1; BAD18544)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="T -> I (in Ref. 1; BAD18544)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="A -> V (in Ref. 4; AAH47378)"
FT /evidence="ECO:0000305"
FT CONFLICT 790
FT /note="T -> A (in Ref. 1; BAD18667)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="P -> R (in Ref. 4; AAH47378)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="P -> H (in Ref. 4; AAH47378)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324
FT /note="P -> R (in Ref. 4; AAH47378)"
FT /evidence="ECO:0000305"
FT CONFLICT 1360
FT /note="K -> E (in Ref. 4; AAH47378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1374 AA; 144569 MW; AD46BD688AF7103E CRC64;
MSSSFFNPSF AFSSHFDPDG APLSELSWPS SLAVVAVSFS GLFAVIVLML ACLCCKKGGI
GFKEFENAEG DEYAADLAQG SPATAAQNGP DVYVLPLTEV SLPMAKQPGR SVQLLKSTDV
GRHSLLYLKE IGRGWFGKVF LGEVNSGISS AQVVVKELQA SASVQEQMQF LEEVQPYRAL
KHSNLLQCLA QCAEVTPYLL VMEFCPLGDL KGYLRSCRVA ESMAPDPRTL QRMACEVACG
VLHLHRNNFV HSDLALRNCL LTADLTVKIG DYGLAHCKYR EDYFVTADQL WVPLRWIAPE
LVDEVHSNLL VVDQTKSGNV WSLGVTIWEL FELGTQPYPQ HSDQQVLAYT VREQQLKLPK
PQLQLTLSDR WYEVMQFCWL QPEQRPTAEE VHLLLSYLCA KGATEAEEEF ERRWRSLRPG
GGGVGPGPGA AGPMLGGVVE LAAASSFPLL EQFAGDGFHA DGDDVLTVTE TSRGLNFEYK
WEAGRGAEAF PATLSPGRTA RLQELCAPDG APPGVVPVLS AHSPSLGSEY FIRLEEAAPA
AGHDPDCAGC APSPPATADQ DDDSDGSTAA SLAMEPLLGH GPPVDVPWGR GDHYPRRSLA
RDPLCPSRSP SPSAGPLSLA EGGAEDADWG VAAFCPAFFE DPLGTSPLGS SGAPPLPLTG
EDELEEVGAR RAAQRGHWRS NVSANNNSGS RCPESWDPVS AGGHAEGCPS PKQTPRASPE
PGYPGEPLLG LQAASAQEPG CCPGLPHLCS AQGLAPAPCL VTPSWTETAS SGGDHPQAEP
KLATEAEGTT GPRLPLPSVP SPSQEGAPLP SEEASAPDAP DALPDSPTPA TGGEVSAIKL
ASALNGSSSS PEVEAPSSED EDTAEATSGI FTDTSSDGLQ ARRPDVVPAF RSLQKQVGTP
DSLDSLDIPS SASDGGYEVF SPSATGPSGG QPRALDSGYD TENYESPEFV LKEAQEGCEP
QAFAELASEG EGPGPETRLS TSLSGLNEKN PYRDSAYFSD LEAEAEATSG PEKKCGGDRA
PGPELGLPST GQPSEQVCLR PGVSGEAQGS GPGEVLPPLL QLEGSSPEPS TCPSGLVPEP
PEPQGPAKVR PGPSPSCSQF FLLTPVPLRS EGNSSEFQGP PGLLSGPAPQ KRMGGPGTPR
APLRLALPGL PAALEGRPEE EEEDSEDSDE SDEELRCYSV QEPSEDSEEE APAVPVVVAE
SQSARNLRSL LKMPSLLSET FCEDLERKKK AVSFFDDVTV YLFDQESPTR ELGEPFPGAK
ESPPTFLRGS PGSPSAPNRP QQADGSPNGS TAEEGGGFAW DDDFPLMTAK AAFAMALDPA
APAPAAPTPT PAPFSRFTVS PAPTSRFSIT HVSDSDAESK RGPEAGAGGE SKEA
