PLPL7_HUMAN
ID PLPL7_HUMAN Reviewed; 1317 AA.
AC Q6ZV29; B5MDD3; Q5T364; Q658X0; Q658Y3; Q6ZTS1; Q86YU8; Q8TAY5; Q96N75;
AC Q9H7N5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 7;
DE EC=3.1.1.- {ECO:0000250|UniProtKB:A2AJ88};
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:A2AJ88};
GN Name=PNPLA7; Synonyms=C9orf111;
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 1 AND 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1016-1268 (ISOFORM 4), AND VARIANT ASN-1050.
RC TISSUE=Liver, Spleen, Thalamus, and Trachea;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 688-1317 (ISOFORM 1), AND VARIANT
RP LEU-908.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1317 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 897-1317 (ISOFORM 3).
RC TISSUE=Lymph node, and 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Lysophospholipase which preferentially deacylates unsaturated
CC lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Also
CC can deacylate, to a lesser extent, lysophosphatidylethanolamine
CC (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid
CC (C16:0). {ECO:0000250|UniProtKB:A2AJ88}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:57597;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A2AJ88}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:A2AJ88}. Lipid droplet
CC {ECO:0000250|UniProtKB:A2AJ88}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6ZV29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZV29-2; Sequence=VSP_026500, VSP_026501, VSP_026502;
CC Name=3;
CC IsoId=Q6ZV29-3; Sequence=VSP_026503;
CC Name=4;
CC IsoId=Q6ZV29-4; Sequence=VSP_026504, VSP_026505;
CC Name=5;
CC IsoId=Q6ZV29-5; Sequence=VSP_026500;
CC -!- DOMAIN: The 3 cNMP binding domains are required for localization to the
CC endoplasmic reticulum. The cNMP binding domain 3 is involved in the
CC binding to lipid droplets. {ECO:0000250|UniProtKB:A2AJ88}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71033.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024443; BAB15733.1; -; mRNA.
DR EMBL; AK055880; BAB71033.1; ALT_INIT; mRNA.
DR EMBL; AK122590; BAC56931.1; -; mRNA.
DR EMBL; AK125060; BAC86036.1; -; mRNA.
DR EMBL; AK126267; BAC86509.1; -; mRNA.
DR EMBL; AL365502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025663; AAH25663.1; -; mRNA.
DR EMBL; AL832944; CAH56322.1; -; mRNA.
DR EMBL; AL832856; CAH56483.1; -; mRNA.
DR CCDS; CCDS48070.1; -. [Q6ZV29-5]
DR CCDS; CCDS7045.1; -. [Q6ZV29-1]
DR RefSeq; NP_001092007.2; NM_001098537.2. [Q6ZV29-5]
DR RefSeq; NP_689499.4; NM_152286.4. [Q6ZV29-1]
DR AlphaFoldDB; Q6ZV29; -.
DR SMR; Q6ZV29; -.
DR BioGRID; 131999; 6.
DR STRING; 9606.ENSP00000384610; -.
DR iPTMnet; Q6ZV29; -.
DR PhosphoSitePlus; Q6ZV29; -.
DR BioMuta; PNPLA7; -.
DR DMDM; 296452996; -.
DR EPD; Q6ZV29; -.
DR jPOST; Q6ZV29; -.
DR MassIVE; Q6ZV29; -.
DR MaxQB; Q6ZV29; -.
DR PaxDb; Q6ZV29; -.
DR PeptideAtlas; Q6ZV29; -.
DR PRIDE; Q6ZV29; -.
DR ProteomicsDB; 68378; -. [Q6ZV29-1]
DR ProteomicsDB; 68379; -. [Q6ZV29-2]
DR ProteomicsDB; 68380; -. [Q6ZV29-3]
DR ProteomicsDB; 68381; -. [Q6ZV29-4]
DR ProteomicsDB; 68382; -. [Q6ZV29-5]
DR Antibodypedia; 2428; 10 antibodies from 8 providers.
DR DNASU; 375775; -.
DR Ensembl; ENST00000277531.8; ENSP00000277531.4; ENSG00000130653.16. [Q6ZV29-1]
DR Ensembl; ENST00000406427.6; ENSP00000384610.1; ENSG00000130653.16. [Q6ZV29-5]
DR GeneID; 375775; -.
DR KEGG; hsa:375775; -.
DR MANE-Select; ENST00000406427.6; ENSP00000384610.1; NM_001098537.3; NP_001092007.2. [Q6ZV29-5]
DR UCSC; uc004cnf.3; human. [Q6ZV29-1]
DR CTD; 375775; -.
DR DisGeNET; 375775; -.
DR GeneCards; PNPLA7; -.
DR HGNC; HGNC:24768; PNPLA7.
DR HPA; ENSG00000130653; Low tissue specificity.
DR MIM; 612122; gene.
DR neXtProt; NX_Q6ZV29; -.
DR OpenTargets; ENSG00000130653; -.
DR PharmGKB; PA134935962; -.
DR VEuPathDB; HostDB:ENSG00000130653; -.
DR eggNOG; KOG2968; Eukaryota.
DR GeneTree; ENSGT00940000156763; -.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; Q6ZV29; -.
DR OMA; FTMNFTT; -.
DR OrthoDB; 253518at2759; -.
DR PhylomeDB; Q6ZV29; -.
DR TreeFam; TF300519; -.
DR PathwayCommons; Q6ZV29; -.
DR Reactome; R-HSA-6814848; Glycerophospholipid catabolism.
DR BioGRID-ORCS; 375775; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; PNPLA7; human.
DR GenomeRNAi; 375775; -.
DR Pharos; Q6ZV29; Tdark.
DR PRO; PR:Q6ZV29; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6ZV29; protein.
DR Bgee; ENSG00000130653; Expressed in left ovary and 97 other tissues.
DR ExpressionAtlas; Q6ZV29; baseline and differential.
DR Genevisible; Q6ZV29; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 3.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1317
FT /note="Patatin-like phospholipase domain-containing protein
FT 7"
FT /id="PRO_0000293489"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..1317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 928..1094
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 320..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..945
FT /note="Involved in the binding to lipid droplets"
FT /evidence="ECO:0000250|UniProtKB:A2AJ88"
FT REGION 1271..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 932..937
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 959..963
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1081..1083
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 320..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 961
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1081
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 145..272
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 458..563
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT BINDING 591..696
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AJ88"
FT MOD_RES 1262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BK26"
FT VAR_SEQ 10
FT /note="Q -> QADFCLGTALHSWGLWFTEEGSPSTM (in isoform 2 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026500"
FT VAR_SEQ 384..433
FT /note="GGPGSATSDLGMACDRARVFLHSDEHPGSSVASKSRKSVMVAEIPSTVSQ
FT -> ARVLCLLPQCLGGLPPTDTSVYSSASSDCCGCSMPVLCIMGHKPHVTVDT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026501"
FT VAR_SEQ 434..1317
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026502"
FT VAR_SEQ 1191..1255
FT /note="EVGYQHGRTVFDIWGRSGVLEKMLRDQQGPSKKPASAVLTCPNASFTDLAEI
FT VSRIEPAKPAMVD -> VP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026503"
FT VAR_SEQ 1256..1268
FT /note="DESDYQTEYEEEL -> GEWRRKTKPWRRA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026504"
FT VAR_SEQ 1269..1317
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026505"
FT VARIANT 236
FT /note="R -> H (in dbSNP:rs12788)"
FT /id="VAR_061139"
FT VARIANT 286
FT /note="G -> S (in dbSNP:rs2298171)"
FT /id="VAR_055696"
FT VARIANT 323
FT /note="R -> Q (in dbSNP:rs11137410)"
FT /id="VAR_033060"
FT VARIANT 364
FT /note="Q -> E (in dbSNP:rs3750378)"
FT /id="VAR_033061"
FT VARIANT 368
FT /note="E -> D (in dbSNP:rs3750379)"
FT /id="VAR_033062"
FT VARIANT 387
FT /note="G -> S (in dbSNP:rs11791683)"
FT /id="VAR_060409"
FT VARIANT 803
FT /note="A -> V (in dbSNP:rs1891630)"
FT /id="VAR_033063"
FT VARIANT 824
FT /note="V -> M (in dbSNP:rs34938599)"
FT /id="VAR_033064"
FT VARIANT 908
FT /note="P -> L (in dbSNP:rs3812499)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033065"
FT VARIANT 993
FT /note="L -> M (in dbSNP:rs35177111)"
FT /id="VAR_033066"
FT VARIANT 1050
FT /note="D -> N (in dbSNP:rs4962237)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_055697"
FT CONFLICT 173
FT /note="F -> L (in Ref. 1; BAC86509)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="K -> M (in Ref. 1; BAC86036)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..399
FT /note="Missing (in Ref. 1; BAC86509)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..473
FT /note="FLHSDEHPGSSVASKSRKSVMVAEIPSTVSQHSESHTDETLASRKSDAIFRA
FT AKKDLLTLMKLEDSSLLDG -> LCLLPQCLGGLPPTDTSVYSSASSDCCGCSMPVLCI
FT MGHKPHVTVDT (in Ref. 1; BAC86509)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="H -> D (in Ref. 1; BAC86036)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="W -> S (in Ref. 1; BAB71033)"
FT /evidence="ECO:0000305"
FT CONFLICT 892..896
FT /note="SLPKL -> RLLPQ (in Ref. 1; BAC56931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016..1027
FT /note="SIFSVFKDQQIE -> WERAHLSPVRPQ (in Ref. 1; BAB15733)"
FT /evidence="ECO:0000305"
FT CONFLICT 1027
FT /note="E -> EQ (in Ref. 4; CAH56483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055
FT /note="W -> R (in Ref. 1; BAB15733/BAB71033/BAC56931/
FT BAC86036, 3; AAH25663 and 4; CAH56322/CAH56483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="V -> VV (in Ref. 4; CAH56483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1317 AA; 145705 MW; 3C0DFC7DE916F349 CRC64;
MEEEKDDSPQ LTGIAVGALL ALALVGVLIL FMFRRLRQFR QAQPTPQYRF RKRDKVMFYG
RKIMRKVTTL PNTLVENTAL PRQRARKRTK VLSLAKRILR FKKEYPALQP KEPPPSLLEA
DLTEFDVKNS HLPSEVLYML KNVRVLGHFE KPLFLELCKH IVFVQLQEGE HVFQPREPDP
SICVVQDGRL EVCIQDTDGT EVVVKEVLAG DSVHSLLSIL DIITGHAAPY KTVSVRAAIP
STILRLPAAA FHGVFEKYPE TLVRVVQIIM VRLQRVTFLA LHNYLGLTTE LFNAESQAIP
LVSVASVAAG KAKKQVFYGE EERLKKPPRL QESCDSDHGG GRPAAAGPLL KRSHSVPAPS
IRKQILEELE KPGAGDPDPS APQGGPGSAT SDLGMACDRA RVFLHSDEHP GSSVASKSRK
SVMVAEIPST VSQHSESHTD ETLASRKSDA IFRAAKKDLL TLMKLEDSSL LDGRVALLHV
PAGTVVSRQG DQDASILFVV SGLLHVYQRK IGSQEDTCLF LTRPGEMVGQ LAVLTGEPLI
FTVKANRDCS FLSISKAHFY EIMRKQPTVV LGVAHTVVKR MSSFVRQIDF ALDWVEVEAG
RAIYRQGDKS DCTYIMLSGR LRSVIRKDDG KKRLAGEYGR GDLVGVVETL THQARATTVH
AVRDSELAKL PAGALTSIKR RYPQVVTRLI HLLGEKILGS LQQGPVTGHQ LGLPTEGSKW
DLGNPAVNLS TVAVMPVSEE VPLTAFALEL EHALSAIGPT LLLTSDNIKR RLGSAALDSV
HEYRLSSWLG QQEDTHRIVL YQADGTLTPW TQRCVRQADC ILIVGLGDQE PTVGELERML
ESTAVRAQKQ LILLHREEGP APARTVEWLN MRSWCSGHLH LCCPRRVFSR RSLPKLVEMY
KHVFQRPPDR HSDFSRLARV LTGNAIALVL GGGGARGCAQ VGVLKALAEC GIPVDMVGGT
SIGAFVGALY SEERNYSQMR IRAKQWAEGM TSLMKAALDL TYPITSMFSG AGFNSSIFSV
FKDQQIEDLW IPYFAITTDI TASAMRVHTD GSLWWYVRAS MSLSGYMPPL CDPKDGHLLM
DGGYINNLPA DVARSMGAKV VIAIDVGSRD ETDLTNYGDA LSGWWLLWKR WNPLATKVKV
LNMAEIQTRL AYVCCVRQLE VVKSSDYCEY LRPPIDSYST LDFGKFNEIC EVGYQHGRTV
FDIWGRSGVL EKMLRDQQGP SKKPASAVLT CPNASFTDLA EIVSRIEPAK PAMVDDESDY
QTEYEEELLD VPRDAYADFQ STSAQQGSDL EDESSLRHRH PSLAFPKLSE GSSDQDG
