ZN365_HUMAN
ID ZN365_HUMAN Reviewed; 407 AA.
AC Q70YC5; A8K0F0; O94930; Q05D75; Q5HYE6; Q68SG8; Q6NSK2; Q6P9D4; Q70YC6;
AC Q70YC7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein ZNF365;
DE AltName: Full=DISC1-binding zinc-finger protein {ECO:0000303|PubMed:17389905};
DE AltName: Full=Protein su48;
GN Name=ZNF365; Synonyms=DBZ {ECO:0000303|PubMed:17389905}, KIAA0844;
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 [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-337, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=12740763; DOI=10.1086/375628;
RA Gianfrancesco F., Esposito T., Ombra M.N., Forabosco P., Maninchedda G.,
RA Fattorini M., Casula S., Vaccargiu S., Casu G., Cardia F., Deiana I.,
RA Melis P., Falchi M., Pirastu M.;
RT "Identification of a novel gene and a common variant associated with uric
RT acid nephrolithiasis in a Sardinian genetic isolate.";
RL Am. J. Hum. Genet. 72:1479-1491(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-337.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-337.
RC TISSUE=Brain, and Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT SER-337.
RC TISSUE=Cervix;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-394 (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-247.
RA Anitha A., Nakamura K., Mori N.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=15363853; DOI=10.1016/j.gene.2004.06.030;
RA Gianfrancesco F., Esposito T., Casu G., Maninchedda G., Roberto R.,
RA Parastu M.;
RT "Emergence of talanin protein associated with human uric acid
RT nephrolithiasis in the hominidae lineage.";
RL Gene 339:131-138(2004).
RN [9]
RP INTERACTION WITH NDE1 AND NDEL1.
RX PubMed=16682949; DOI=10.1038/sj.onc.1209637;
RA Hirohashi Y., Wang Q., Liu Q., Li B., Du X., Zhang H., Furuuchi K.,
RA Masuda K., Sato N., Greene M.I.;
RT "Centrosomal proteins Nde1 and Su48 form a complex regulated by
RT phosphorylation.";
RL Oncogene 25:6048-6055(2006).
RN [10]
RP HOMODIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=16617106; DOI=10.1073/pnas.0601682103;
RA Wang Q., Du X., Meinkoth J., Hirohashi Y., Zhang H., Liu Q., Richter M.,
RA Greene M.I.;
RT "Characterization of Su48, a centrosome protein essential for cell
RT division.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6512-6517(2006).
RN [11]
RP FUNCTION, INTERACTION WITH DISC1, AND TISSUE SPECIFICITY.
RX PubMed=17389905; DOI=10.1038/sj.mp.4001945;
RA Hattori T., Baba K., Matsuzaki S., Honda A., Miyoshi K., Inoue K.,
RA Taniguchi M., Hashimoto H., Shintani N., Baba A., Shimizu S., Yukioka F.,
RA Kumamoto N., Yamaguchi A., Tohyama M., Katayama T.;
RT "A novel DISC1-interacting partner DISC1-binding zinc-finger protein:
RT implication in the modulation of DISC1-dependent neurite outgrowth.";
RL Mol. Psychiatry 12:398-407(2007).
RN [12]
RP FUNCTION.
RX PubMed=23776040; DOI=10.1158/2159-8290.cd-12-0536;
RA Zhang Y., Shin S.J., Liu D., Ivanova E., Foerster F., Ying H., Zheng H.,
RA Xiao Y., Chen Z., Protopopov A., Depinho R.A., Paik J.H.;
RT "ZNF365 promotes stability of fragile sites and telomeres.";
RL Cancer Discov. 3:798-811(2013).
RN [13]
RP FUNCTION, INTERACTION WITH PARP1, AND INDUCTION.
RX PubMed=23966166; DOI=10.4161/cc.25882;
RA Zhang Y., Park E., Kim C.S., Paik J.H.;
RT "ZNF365 promotes stalled replication forks recovery to maintain genome
RT stability.";
RL Cell Cycle 12:2817-2828(2013).
CC -!- FUNCTION: Involved in the regulation of neurogenesis. Negatively
CC regulates neurite outgrowth (PubMed:17389905). Involved in the
CC morphogenesis of basket cells in the somatosensory cortex during
CC embryogenesis. Involved in the positive regulation of oligodendrocyte
CC differentiation during postnatal growth. Involved in dendritic
CC arborization, morphogenesis of spine density dendrite, and
CC establishment of postsynaptic dendrite density in cortical pyramidal
CC neurons (By similarity). Involved in homologous recombination (HR)
CC repair pathway. Required for proper resolution of DNA double-strand
CC breaks (DSBs) by HR. Is required for recovery of stalled replication
CC forks, and directly contributes to genomic stability. Interacts with
CC PARP1 and mediates MRE11-dependent DNA end resection during replication
CC fork recovery (PubMed:23966166). Contributes to genomic stability by
CC preventing telomere dysfunction (PubMed:23776040).
CC {ECO:0000250|UniProtKB:Q8BG89, ECO:0000269|PubMed:17389905,
CC ECO:0000269|PubMed:23776040, ECO:0000269|PubMed:23966166}.
CC -!- SUBUNIT: Homodimer. Interacts with NDE1 and NDEL1. Does not interact
CC with TUBG1. Interacts with DISC1 (PubMed:17389905). Interacts with
CC PARP1 (PubMed:23966166). {ECO:0000269|PubMed:16682949,
CC ECO:0000269|PubMed:17389905, ECO:0000269|PubMed:23966166}.
CC -!- INTERACTION:
CC Q70YC5; Q9NXR1: NDE1; NbExp=3; IntAct=EBI-941182, EBI-941227;
CC Q70YC5-1; Q70YC5-1: ZNF365; NbExp=4; IntAct=EBI-15580061, EBI-15580061;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:16617106}. Note=localizes to the
CC centrosome at all stages of the cell cycle.
CC {ECO:0000269|PubMed:16617106}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=ZNF365A;
CC IsoId=Q70YC5-1; Sequence=Displayed;
CC Name=2; Synonyms=ZNF365B;
CC IsoId=Q70YC5-2; Sequence=VSP_016599, VSP_016600;
CC Name=3; Synonyms=ZNF365C;
CC IsoId=Q70YC5-3; Sequence=VSP_016598;
CC Name=5;
CC IsoId=Q70YC5-4; Sequence=VSP_016597;
CC Name=6;
CC IsoId=Q70YC5-5; Sequence=VSP_016596;
CC Name=4; Synonyms=Talanin, ZNF365D;
CC IsoId=Q70YC4-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain. Isoform 2 is
CC expressed in placenta and at low level in lung and liver. Isoform 3 is
CC expressed in kidney and pancreas. Isoform 1 is expressed exclusively in
CC brain (PubMed:17389905). {ECO:0000269|PubMed:12740763,
CC ECO:0000269|PubMed:17389905}.
CC -!- INDUCTION: Induced by gamma irradiation and zeocin.
CC {ECO:0000269|PubMed:23966166}.
CC -!- MISCELLANEOUS: Cells silencing ZNF365 display delayed mitotic
CC progression and exit, due to increased replication stress, and
CC ultimately leading to cytokinesis failure, re-duplication of
CC centrosomes and increased aneuploidy. {ECO:0000269|PubMed:23966166}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17841.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA74867.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ505147; CAD43726.1; -; mRNA.
DR EMBL; AJ505148; CAD43727.1; -; mRNA.
DR EMBL; AJ505149; CAD43728.1; -; mRNA.
DR EMBL; AB020651; BAA74867.2; ALT_INIT; mRNA.
DR EMBL; AK289515; BAF82204.1; -; mRNA.
DR EMBL; AK289808; BAF82497.1; -; mRNA.
DR EMBL; BX647904; CAI46100.1; -; mRNA.
DR EMBL; AC024597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017841; AAH17841.1; ALT_SEQ; mRNA.
DR EMBL; BC035049; AAH35049.1; -; mRNA.
DR EMBL; BC060817; AAH60817.1; -; mRNA.
DR EMBL; AY547355; AAT27443.1; -; Genomic_DNA.
DR CCDS; CCDS31209.1; -. [Q70YC5-1]
DR CCDS; CCDS41531.1; -. [Q70YC5-2]
DR RefSeq; NP_055766.2; NM_014951.2. [Q70YC5-1]
DR RefSeq; NP_955522.1; NM_199450.2. [Q70YC5-2]
DR RefSeq; NP_955523.1; NM_199451.2.
DR AlphaFoldDB; Q70YC5; -.
DR SMR; Q70YC5; -.
DR BioGRID; 116557; 13.
DR CORUM; Q70YC5; -.
DR DIP; DIP-35261N; -.
DR IntAct; Q70YC5; 4.
DR STRING; 9606.ENSP00000387091; -.
DR iPTMnet; Q70YC5; -.
DR PhosphoSitePlus; Q70YC5; -.
DR BioMuta; ZNF365; -.
DR DMDM; 317373495; -.
DR MassIVE; Q70YC5; -.
DR MaxQB; Q70YC5; -.
DR PeptideAtlas; Q70YC5; -.
DR PRIDE; Q70YC5; -.
DR ProteomicsDB; 68572; -. [Q70YC5-1]
DR ProteomicsDB; 68573; -. [Q70YC5-2]
DR ProteomicsDB; 68574; -. [Q70YC5-3]
DR ProteomicsDB; 68575; -. [Q70YC5-4]
DR ProteomicsDB; 68576; -. [Q70YC5-5]
DR Antibodypedia; 28272; 428 antibodies from 20 providers.
DR DNASU; 22891; -.
DR Ensembl; ENST00000395254.8; ENSP00000378674.3; ENSG00000138311.18. [Q70YC5-1]
DR Ensembl; ENST00000395255.7; ENSP00000378675.3; ENSG00000138311.18. [Q70YC5-2]
DR GeneID; 22891; -.
DR KEGG; hsa:22891; -.
DR MANE-Select; ENST00000395254.8; ENSP00000378674.3; NM_014951.3; NP_055766.2.
DR UCSC; uc001jlz.5; human. [Q70YC5-1]
DR CTD; 22891; -.
DR DisGeNET; 22891; -.
DR GeneCards; ZNF365; -.
DR HGNC; HGNC:18194; ZNF365.
DR HPA; ENSG00000138311; Tissue enhanced (brain, esophagus).
DR MalaCards; ZNF365; -.
DR MIM; 607818; gene.
DR neXtProt; NX_Q70YC5; -.
DR OpenTargets; ENSG00000138311; -.
DR Orphanet; 2073; Narcolepsy type 1.
DR Orphanet; 83465; Narcolepsy type 2.
DR PharmGKB; PA134873576; -.
DR VEuPathDB; HostDB:ENSG00000138311; -.
DR eggNOG; ENOG502QT88; Eukaryota.
DR GeneTree; ENSGT00530000063713; -.
DR HOGENOM; CLU_049609_0_0_1; -.
DR InParanoid; Q70YC5; -.
DR OMA; AKPHSFQ; -.
DR OrthoDB; 918236at2759; -.
DR PhylomeDB; Q70YC5; -.
DR TreeFam; TF329439; -.
DR PathwayCommons; Q70YC5; -.
DR SignaLink; Q70YC5; -.
DR BioGRID-ORCS; 22891; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; ZNF365; human.
DR GenomeRNAi; 22891; -.
DR Pharos; Q70YC5; Tbio.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q70YC5; protein.
DR Bgee; ENSG00000138311; Expressed in middle temporal gyrus and 143 other tissues.
DR ExpressionAtlas; Q70YC5; baseline and differential.
DR Genevisible; Q70YC5; HS.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0021687; P:cerebellar molecular layer morphogenesis; ISS:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; ISS:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0110026; P:regulation of DNA strand resection involved in replication fork processing; IMP:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding;
KW Neurogenesis; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..407
FT /note="Protein ZNF365"
FT /id="PRO_0000076374"
FT ZN_FING 26..51
FT /note="C2H2-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 347..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..297
FT /evidence="ECO:0000255"
FT COMPBIAS 347..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQS2"
FT VAR_SEQ 1..356
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016596"
FT VAR_SEQ 1
FT /note="M -> MTMRPPQSCEPTFRVM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016597"
FT VAR_SEQ 309..407
FT /note="LTDISSNRKPKCLSRGHPHSVCNHPDLKAHFHPKGRNHLKKAKDDRASMQPA
FT KAIHEQAESSRDLCRPPKKGELLGFGRKGNIRPKMAKKKPTAIVNII -> SWKGAGEA
FT RLVCQNDLELEIFGHINHHLSGLKDSHCLVFLQAPPVPWIILASFLWILGNPWTSSTAT
FT AGFSQIWVLFPFCGGTFHHNEKDVLGLQDFERESVSTSQSRNISLLTLGQLQNCVIGKL
FT TIIDLLTEHLLGVRHGVICFPWGLPSSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12740763"
FT /id="VSP_016598"
FT VAR_SEQ 309..333
FT /note="LTDISSNRKPKCLSRGHPHSVCNHP -> SWKGAGEARLVCQNDLELEESAI
FT VE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12740763"
FT /id="VSP_016599"
FT VAR_SEQ 334..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12740763"
FT /id="VSP_016600"
FT VARIANT 337
FT /note="A -> S (in dbSNP:rs3758490)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:12740763, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_024325"
FT CONFLICT 55
FT /note="E -> Q (in Ref. 7; AAT27443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46542 MW; CC3C25AF6A753E64 CRC64;
MQQKAFEESR YPWQESFENV AVCLPLRCPR CGDHTRFRSL SSLRAHLEFS HSYEERTLLT
KCSLFPSLKD TDLVTSSELL KPGKLQSSGN VVKQKPSYVN LYSISHEHSK DRKPFEVVAE
RPVSYVQTYT AMDLHADSLD GTRSGPGLPT SDTKASFEAH VREKFNRMVE AVDRTIEKRI
DKLTKELAQK TAELLEVRAA FVQLTQKKQE VQRRERALNR QVDVAVEMIA VLRQRLTESE
EELLRKEEEV VTFNHFLEAA AEKEVQGKAR LQDFIENLLQ RVELAEKQLE YYQSQQASGF
VRDLSGHVLT DISSNRKPKC LSRGHPHSVC NHPDLKAHFH PKGRNHLKKA KDDRASMQPA
KAIHEQAESS RDLCRPPKKG ELLGFGRKGN IRPKMAKKKP TAIVNII
