ID WWC2_HUMAN Reviewed; 1192 AA.
AC Q6AWC2; Q32Q84; Q69YQ1; Q6AWB8; Q6ZSY9; Q6ZU09; Q7Z620; Q8TEB8; Q9H6P0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Protein WWC2;
DE AltName: Full=BH-3-only member B;
DE AltName: Full=WW domain-containing protein 2;
GN Name=WWC2; Synonyms=BOMB;
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 3 AND 5), AND VARIANT
RP HIS-904.
RC TISSUE=Brain;
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] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 698-1192 (ISOFORM 6), AND VARIANTS PHE-816; HIS-904
RP AND THR-1189.
RC TISSUE=Fetal kidney, Lung endothelial cell, and Melanoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 408-879 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP MRNA] OF 415-1192 (ISOFORM 4), AND VARIANTS SER-773 AND PHE-816.
RC TISSUE=Kidney, and Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 713-1192 (ISOFORM 1).
RA Liu Z., Jiang Z., Hu C.-A.A.;
RT "Novel pro-apoptotic BH-3-only proteins, apolipoprotein L6 (ApoL6) and BH3-
RT only member B (BOMB), by genomics and functional expression approaches in
RT cancer.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH DLC1; PRKCZ;
RP LATS1 AND LATS2.
RX PubMed=24682284; DOI=10.1093/molbev/msu115;
RA Wennmann D.O., Schmitz J., Wehr M.C., Krahn M.P., Koschmal N.,
RA Gromnitza S., Schulze U., Weide T., Chekuri A., Skryabin B.V., Gerke V.,
RA Pavenstadt H., Duning K., Kremerskothen J.;
RT "Evolutionary and Molecular Facts Link the WWC Protein Family to Hippo
RT Signaling.";
RL Mol. Biol. Evol. 31:1710-1723(2014).
CC -!- FUNCTION: Negative regulator of the Hippo signaling pathway, also known
CC as the Salvador-Warts-Hippo (SWH) pathway. Enhances phosphorylation of
CC LATS1 and YAP1 and negatively regulates cell proliferation and organ
CC growth due to a suppression of the transcriptional activity of YAP1,
CC the major effector of the Hippo pathway. {ECO:0000269|PubMed:24682284}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with WWC1 and WWC3.
CC Interacts with DLC1 and PRKCZ. Interacts (via WW domains) with LATS1
CC and LATS2. {ECO:0000269|PubMed:24682284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24682284}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q6AWC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AWC2-2; Sequence=VSP_029215;
CC Name=3;
CC IsoId=Q6AWC2-3; Sequence=VSP_029214;
CC Name=4;
CC IsoId=Q6AWC2-4; Sequence=VSP_029217;
CC Name=5;
CC IsoId=Q6AWC2-5; Sequence=VSP_029216, VSP_029218;
CC Name=6;
CC IsoId=Q6AWC2-6; Sequence=VSP_029219;
CC Name=7;
CC IsoId=Q6AWC2-7; Sequence=VSP_029213;
CC -!- SIMILARITY: Belongs to the WWC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17957.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI07684.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB15215.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB85032.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97477.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK025682; BAB15215.1; ALT_INIT; mRNA.
DR EMBL; AK074260; BAB85032.1; ALT_INIT; mRNA.
DR EMBL; AK126057; BAC86418.1; -; mRNA.
DR EMBL; AK127061; BAC86807.1; -; mRNA.
DR EMBL; BX647378; CAH10569.1; -; mRNA.
DR EMBL; BX647704; CAH10570.1; -; mRNA.
DR EMBL; AL832424; CAH10641.1; -; mRNA.
DR EMBL; AC093844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017957; AAH17957.1; ALT_INIT; mRNA.
DR EMBL; BC053873; AAH53873.2; -; mRNA.
DR EMBL; BC107683; AAI07684.1; ALT_SEQ; mRNA.
DR EMBL; AJ566366; CAD97477.1; ALT_INIT; mRNA.
DR CCDS; CCDS34109.2; -. [Q6AWC2-1]
DR CCDS; CCDS93674.1; -. [Q6AWC2-6]
DR RefSeq; NP_079225.5; NM_024949.5. [Q6AWC2-1]
DR RefSeq; XP_011530571.1; XM_011532269.2.
DR AlphaFoldDB; Q6AWC2; -.
DR SMR; Q6AWC2; -.
DR BioGRID; 123070; 29.
DR IntAct; Q6AWC2; 15.
DR MINT; Q6AWC2; -.
DR STRING; 9606.ENSP00000384222; -.
DR GlyGen; Q6AWC2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6AWC2; -.
DR PhosphoSitePlus; Q6AWC2; -.
DR BioMuta; WWC2; -.
DR DMDM; 160358940; -.
DR EPD; Q6AWC2; -.
DR jPOST; Q6AWC2; -.
DR MassIVE; Q6AWC2; -.
DR MaxQB; Q6AWC2; -.
DR PaxDb; 9606-ENSP00000384222; -.
DR PeptideAtlas; Q6AWC2; -.
DR ProteomicsDB; 66193; -. [Q6AWC2-1]
DR ProteomicsDB; 66194; -. [Q6AWC2-2]
DR ProteomicsDB; 66195; -. [Q6AWC2-3]
DR ProteomicsDB; 66196; -. [Q6AWC2-4]
DR ProteomicsDB; 66197; -. [Q6AWC2-5]
DR ProteomicsDB; 66198; -. [Q6AWC2-6]
DR ProteomicsDB; 66199; -. [Q6AWC2-7]
DR Pumba; Q6AWC2; -.
DR Antibodypedia; 51479; 65 antibodies from 18 providers.
DR CPTC; Q6AWC2; 3 antibodies.
DR DNASU; 80014; -.
DR Ensembl; ENST00000403733.8; ENSP00000384222.3; ENSG00000151718.16. [Q6AWC2-1]
DR Ensembl; ENST00000438543.5; ENSP00000413521.1; ENSG00000151718.16. [Q6AWC2-5]
DR Ensembl; ENST00000448232.6; ENSP00000398577.2; ENSG00000151718.16. [Q6AWC2-6]
DR Ensembl; ENST00000504005.5; ENSP00000427569.1; ENSG00000151718.16. [Q6AWC2-3]
DR Ensembl; ENST00000508747.1; ENSP00000420835.1; ENSG00000151718.16. [Q6AWC2-7]
DR Ensembl; ENST00000513834.5; ENSP00000425054.1; ENSG00000151718.16. [Q6AWC2-4]
DR GeneID; 80014; -.
DR KEGG; hsa:80014; -.
DR MANE-Select; ENST00000403733.8; ENSP00000384222.3; NM_024949.6; NP_079225.5.
DR UCSC; uc003ivo.5; human. [Q6AWC2-1]
DR AGR; HGNC:24148; -.
DR CTD; 80014; -.
DR DisGeNET; 80014; -.
DR GeneCards; WWC2; -.
DR HGNC; HGNC:24148; WWC2.
DR HPA; ENSG00000151718; Low tissue specificity.
DR MIM; 620110; gene.
DR neXtProt; NX_Q6AWC2; -.
DR OpenTargets; ENSG00000151718; -.
DR PharmGKB; PA143485671; -.
DR VEuPathDB; HostDB:ENSG00000151718; -.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00410000025556; -.
DR HOGENOM; CLU_005420_0_0_1; -.
DR InParanoid; Q6AWC2; -.
DR OMA; DTDYQYK; -.
DR OrthoDB; 1334597at2759; -.
DR PhylomeDB; Q6AWC2; -.
DR TreeFam; TF324040; -.
DR PathwayCommons; Q6AWC2; -.
DR SignaLink; Q6AWC2; -.
DR BioGRID-ORCS; 80014; 12 hits in 1163 CRISPR screens.
DR ChiTaRS; WWC2; human.
DR GenomeRNAi; 80014; -.
DR Pharos; Q6AWC2; Tbio.
DR PRO; PR:Q6AWC2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6AWC2; Protein.
DR Bgee; ENSG00000151718; Expressed in renal medulla and 194 other cell types or tissues.
DR ExpressionAtlas; Q6AWC2; baseline and differential.
DR Genevisible; Q6AWC2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IDA:BHF-UCL.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0035330; P:regulation of hippo signaling; IBA:GO_Central.
DR CDD; cd08680; C2_Kibra; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037771; C2_WWC.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR14791; BOMB/KIRA PROTEINS; 1.
DR PANTHER; PTHR14791:SF26; PROTEIN WWC2; 1.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1192
FT /note="Protein WWC2"
FT /id="PRO_0000309490"
FT DOMAIN 10..43
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 57..90
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 698..821
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1050
FT /note="Interaction with PRKCZ"
FT /evidence="ECO:0000269|PubMed:24682284"
FT REGION 1124..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..194
FT /evidence="ECO:0000255"
FT COILED 224..256
FT /evidence="ECO:0000255"
FT COILED 302..421
FT /evidence="ECO:0000255"
FT COILED 859..887
FT /evidence="ECO:0000255"
FT COILED 1068..1144
FT /evidence="ECO:0000255"
FT COMPBIAS 873..887
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXJ0"
FT MOD_RES 1004
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXJ0"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..895
FT /note="MPRRAGSGQLPLPRGWEEARDYDGKVFYIDHNTRRTSWIDPRDRLTKPLSFA
FT DCVGDELPWGWEAGFDPQIGVYYIDHINKTTQIEDPRKQWRGEQEKMLKDYLSVAQDAL
FT RTQKELYHVKEQRLALALDEYVRLNDAYKEKSSSHTSLFSGSSSSTKYDPDILKAEIST
FT TRLRVKKLKRELSQMKQELLYKEQGFETLQQIDKKMSGGQSGYELSEAKAILTELKSIR
FT KAISSGEKEKQDLMQSLAKLQERFHLDQNIGRSEPDLRCSPVNSHLCLSRQTLDAGSQT
FT SISGDIGVRSRSNLAEKVRLSLQYEEAKRSMANLKIELSKLDSEAWPGALDIEKEKLML
FT INEKEELLKELQFVTPQKRTQDELERLEAERQRLEEELLSVRGTPSRALAERLRLEERR
FT KELLQKLEETTKLTTYLHSQLKSLSASTLSMSSGSSLGSLASSRGSLNTSSRGSLNSLS
FT STELYYSSQSDQIDVDYQYKLDFLLQEKSGYIPSGPITTIHENEVVKSPSQPGQSGLCG
FT VAAAATGHTPPLAEAPKSVASLSSRSSLSSLSPPGSPLVLEGTFPMSSSHDASLHQFTA
FT DFEDCELSSHFADISLIENQILLDSDSGGASQSLSEDKDLNECAREPLYEGTADVEKSL
FT PKRRVIHLLGEKTTCVSAAVSDESVAGDSGVYEAFVKQPSEMEDVTYSEEDVAIVETAQ
FT VQIGLRYNAKSSSFMVIIAQLRNLHAFLIPHTSKVYFRVAVLPSSTDVSCLFRTKVHPP
FT TESILFNDVFRVAISQTALQQKTLRVDLCSVSKHRREECLAGTQISLADLPFSSEVFTL
FT WYNLLPSKQMPCKKNEENEDSVFQPNQPLVDSIDLDAVSALLARTSAELLAVEQELAQE
FT EEEESGQEEPRGPDGDW -> MPRLRVHGACLPTKSVLFLFYHR (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029213"
FT VAR_SEQ 1..318
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029214"
FT VAR_SEQ 1..205
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029215"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029216"
FT VAR_SEQ 588..637
FT /note="CELSSHFADISLIENQILLDSDSGGASQSLSEDKDLNECAREPLYEGTAD
FT -> Y (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029217"
FT VAR_SEQ 786..1192
FT /note="VDLCSVSKHRREECLAGTQISLADLPFSSEVFTLWYNLLPSKQMPCKKNEEN
FT EDSVFQPNQPLVDSIDLDAVSALLARTSAELLAVEQELAQEEEEESGQEEPRGPDGDWL
FT TMLREASDEIVAEKEAEVKLPEDSSCTEDLSSCTSVPEMNEDGNRKESNCAKDLRSQPP
FT TRIPTLVDKETNTDEAANDNMAVRPKERSSLSSRQHPFVRSSVIVRSQTFSPGERNQYI
FT CRLNRSDSDSSTLAKKSLFVRNSTERRSLRVKRTVCQSVLRRTTQECPVRTSLDLELDL
FT QASLTRQSRLNDELQALRDLRQKLEELKAQGETDLPPGVLEDERFQRLLKQAEKQAEQS
FT KEEQKQGLNAEKLMRQVSKDVCRLREQSQKVPRQVQSFREKIAYFTRAKISIPSLPADD
FT V -> KNFTFVTAITHGVCLPLPVPMPSFA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029218"
FT VAR_SEQ 895
FT /note="W -> WLNTYFLCCWELKDDVFTRLTVKPL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029219"
FT VARIANT 773
FT /note="A -> S (in dbSNP:rs11941467)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_036965"
FT VARIANT 816
FT /note="V -> F (in dbSNP:rs11734376)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_036966"
FT VARIANT 904
FT /note="D -> H (in dbSNP:rs3814422)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_036967"
FT VARIANT 979
FT /note="R -> C (in dbSNP:rs45470696)"
FT /id="VAR_062108"
FT VARIANT 1189
FT /note="A -> T (in dbSNP:rs4862155)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_036968"
FT CONFLICT 108
FT /note="Q -> R (in Ref. 1; BAC86418)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="K -> E (in Ref. 1; BAC86418)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="D -> Y (in Ref. 2; CAH10569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1192 AA; 133891 MW; 937D419FF18F62C0 CRC64;
MPRRAGSGQL PLPRGWEEAR DYDGKVFYID HNTRRTSWID PRDRLTKPLS FADCVGDELP
WGWEAGFDPQ IGVYYIDHIN KTTQIEDPRK QWRGEQEKML KDYLSVAQDA LRTQKELYHV
KEQRLALALD EYVRLNDAYK EKSSSHTSLF SGSSSSTKYD PDILKAEIST TRLRVKKLKR
ELSQMKQELL YKEQGFETLQ QIDKKMSGGQ SGYELSEAKA ILTELKSIRK AISSGEKEKQ
DLMQSLAKLQ ERFHLDQNIG RSEPDLRCSP VNSHLCLSRQ TLDAGSQTSI SGDIGVRSRS
NLAEKVRLSL QYEEAKRSMA NLKIELSKLD SEAWPGALDI EKEKLMLINE KEELLKELQF
VTPQKRTQDE LERLEAERQR LEEELLSVRG TPSRALAERL RLEERRKELL QKLEETTKLT
TYLHSQLKSL SASTLSMSSG SSLGSLASSR GSLNTSSRGS LNSLSSTELY YSSQSDQIDV
DYQYKLDFLL QEKSGYIPSG PITTIHENEV VKSPSQPGQS GLCGVAAAAT GHTPPLAEAP
KSVASLSSRS SLSSLSPPGS PLVLEGTFPM SSSHDASLHQ FTADFEDCEL SSHFADISLI
ENQILLDSDS GGASQSLSED KDLNECAREP LYEGTADVEK SLPKRRVIHL LGEKTTCVSA
AVSDESVAGD SGVYEAFVKQ PSEMEDVTYS EEDVAIVETA QVQIGLRYNA KSSSFMVIIA
QLRNLHAFLI PHTSKVYFRV AVLPSSTDVS CLFRTKVHPP TESILFNDVF RVAISQTALQ
QKTLRVDLCS VSKHRREECL AGTQISLADL PFSSEVFTLW YNLLPSKQMP CKKNEENEDS
VFQPNQPLVD SIDLDAVSAL LARTSAELLA VEQELAQEEE EESGQEEPRG PDGDWLTMLR
EASDEIVAEK EAEVKLPEDS SCTEDLSSCT SVPEMNEDGN RKESNCAKDL RSQPPTRIPT
LVDKETNTDE AANDNMAVRP KERSSLSSRQ HPFVRSSVIV RSQTFSPGER NQYICRLNRS
DSDSSTLAKK SLFVRNSTER RSLRVKRTVC QSVLRRTTQE CPVRTSLDLE LDLQASLTRQ
SRLNDELQAL RDLRQKLEEL KAQGETDLPP GVLEDERFQR LLKQAEKQAE QSKEEQKQGL
NAEKLMRQVS KDVCRLREQS QKVPRQVQSF REKIAYFTRA KISIPSLPAD DV
//
