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   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.
DR   Genevisible; Q6AWC2; HS.
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
//