ID   SALL2_HUMAN             Reviewed;        1007 AA.
AC   Q9Y467; B2RMX6; B9EGK8; Q8N656; Q9Y4G1;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 5.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Sal-like protein 2;
DE   AltName: Full=Zinc finger protein 795;
DE   AltName: Full=Zinc finger protein SALL2;
DE   AltName: Full=Zinc finger protein Spalt-2;
DE            Short=Sal-2;
DE            Short=hSal2;
GN   Name=SALL2; Synonyms=KIAA0360, SAL2, ZNF795;
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] (ISOFORM 1).
RC   TISSUE=Fetus;
RX   PubMed=8975705; DOI=10.1006/geno.1996.0631;
RA   Kohlhase J., Schuh R., Dowe G., Kuehnlein R.P., Jaeckle H., Schroeder B.,
RA   Schulz-Schaeffer W., Kretzschmar H.A., Koehler A., Mueller U.,
RA   Raab-Vetter M., Burkhardt E., Engel W., Stick R.;
RT   "Isolation, characterization, and organ-specific expression of two novel
RT   human zinc finger genes related to the Drosophila gene spalt.";
RL   Genomics 38:291-298(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-746.
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
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 GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   PRO-122.
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 541-1005 (ISOFORM 1), AND VARIANT GLY-746.
RA   Morgan J.W., Ford D., Ma Y., Maizel A.L.;
RT   "Homo sapiens mRNA for zinc finger protein, SALL2 exon 2.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   DOMAIN.
RX   PubMed=16545361; DOI=10.1016/j.ydbio.2006.02.009;
RA   Sweetman D., Muensterberg A.;
RT   "The vertebrate spalt genes in development and disease.";
RL   Dev. Biol. 293:285-293(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-911, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18655026; DOI=10.1002/pmic.200700887;
RA   Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J.,
RA   Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
RT   "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell
RT   line Chang liver cells.";
RL   Proteomics 8:2885-2896(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797; SER-802 AND SER-806, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-802 AND SER-806, AND
RP   IDENTIFICATION BY 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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
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   [14]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INVOLVEMENT IN COAR.
RX   PubMed=24412933; DOI=10.1093/hmg/ddt643;
RA   Kelberman D., Islam L., Lakowski J., Bacchelli C., Chanudet E., Lescai F.,
RA   Patel A., Stupka E., Buck A., Wolf S., Beales P.L., Jacques T.S.,
RA   Bitner-Glindzicz M., Liasis A., Lehmann O.J., Kohlhase J., Nischal K.K.,
RA   Sowden J.C.;
RT   "Mutation of SALL2 causes recessive ocular coloboma in humans and mice.";
RL   Hum. Mol. Genet. 23:2511-2526(2014).
CC   -!- FUNCTION: Probable transcription factor that plays a role in eye
CC       development before, during, and after optic fissure closure.
CC       {ECO:0000269|PubMed:24412933}.
CC   -!- INTERACTION:
CC       Q9Y467; Q8TAP6: CEP76; NbExp=4; IntAct=EBI-746180, EBI-742887;
CC       Q9Y467; P08138: NGFR; NbExp=3; IntAct=EBI-746180, EBI-1387782;
CC       Q9Y467; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-746180, EBI-10182121;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y467-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y467-3; Sequence=VSP_056251, VSP_056252, VSP_056253;
CC   -!- TISSUE SPECIFICITY: Highest levels in adult brain (in different areas).
CC       Lower levels in heart; very low levels in kidney and pancreas.
CC       Expressed throughout the retina and lens vesicle as well as the
CC       periocular mesenchyme. {ECO:0000269|PubMed:24412933}.
CC   -!- DEVELOPMENTAL STAGE: In fetal brain exclusively in pontine nuclei.
CC       Expressed at 5 weeks of development, the stage at which optic fissure
CC       closure starts. Expression is maintained in the developing retina up to
CC       8 weeks; after completion of fissure closure, it is restricted to the
CC       inner neuroblastic layer. Expressed in the cornea, lens, and retina at
CC       different developmental stages. {ECO:0000269|PubMed:24412933}.
CC   -!- DISEASE: Coloboma, ocular, autosomal recessive (COAR) [MIM:216820]: An
CC       ocular anomaly resulting from abnormal morphogenesis of the optic cup
CC       and stalk, and incomplete fusion of the fetal intra-ocular fissure
CC       during gestation. The clinical presentation is variable. Some
CC       individuals may present with minimal defects in the anterior iris leaf
CC       without other ocular defects. More complex malformations create a
CC       combination of iris, uveoretinal and/or optic nerve defects without or
CC       with microphthalmia or even anophthalmia.
CC       {ECO:0000269|PubMed:24412933}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA21638.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X98834; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB002358; BAA21638.2; ALT_INIT; mRNA.
DR   EMBL; AE000521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE000658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC024245; AAH24245.1; -; mRNA.
DR   EMBL; BC090958; AAH90958.1; -; mRNA.
DR   EMBL; BC136528; AAI36529.1; -; mRNA.
DR   EMBL; BC136529; AAI36530.1; -; mRNA.
DR   EMBL; AF465630; AAL74188.1; -; mRNA.
DR   CCDS; CCDS32045.1; -. [Q9Y467-1]
DR   RefSeq; NP_001278375.1; NM_001291446.1.
DR   RefSeq; NP_001278376.1; NM_001291447.1.
DR   RefSeq; NP_005398.2; NM_005407.2. [Q9Y467-1]
DR   AlphaFoldDB; Q9Y467; -.
DR   SMR; Q9Y467; -.
DR   BioGRID; 112204; 85.
DR   IntAct; Q9Y467; 30.
DR   MINT; Q9Y467; -.
DR   STRING; 9606.ENSP00000483562; -.
DR   GlyCosmos; Q9Y467; 2 sites, 1 glycan.
DR   GlyGen; Q9Y467; 10 sites, 1 O-linked glycan (10 sites).
DR   iPTMnet; Q9Y467; -.
DR   PhosphoSitePlus; Q9Y467; -.
DR   BioMuta; SALL2; -.
DR   DMDM; 296453020; -.
DR   EPD; Q9Y467; -.
DR   jPOST; Q9Y467; -.
DR   MassIVE; Q9Y467; -.
DR   MaxQB; Q9Y467; -.
DR   PaxDb; 9606-ENSP00000483562; -.
DR   PeptideAtlas; Q9Y467; -.
DR   ProteomicsDB; 72132; -.
DR   ProteomicsDB; 86114; -. [Q9Y467-1]
DR   Pumba; Q9Y467; -.
DR   Antibodypedia; 22191; 116 antibodies from 21 providers.
DR   DNASU; 6297; -.
DR   Ensembl; ENST00000611430.4; ENSP00000484460.1; ENSG00000165821.12. [Q9Y467-3]
DR   Ensembl; ENST00000614342.1; ENSP00000483562.1; ENSG00000165821.12. [Q9Y467-1]
DR   GeneID; 6297; -.
DR   KEGG; hsa:6297; -.
DR   UCSC; uc032atc.2; human. [Q9Y467-1]
DR   AGR; HGNC:10526; -.
DR   CTD; 6297; -.
DR   DisGeNET; 6297; -.
DR   GeneCards; SALL2; -.
DR   HGNC; HGNC:10526; SALL2.
DR   HPA; ENSG00000165821; Tissue enhanced (brain).
DR   MalaCards; SALL2; -.
DR   MIM; 216820; phenotype.
DR   MIM; 602219; gene.
DR   neXtProt; NX_Q9Y467; -.
DR   OpenTargets; ENSG00000165821; -.
DR   Orphanet; 98942; Coloboma of choroid and retina.
DR   Orphanet; 98943; Coloboma of eye lens.
DR   Orphanet; 98946; Coloboma of eyelid.
DR   Orphanet; 98944; Coloboma of iris.
DR   Orphanet; 98945; Coloboma of macula.
DR   Orphanet; 98947; Coloboma of optic disc.
DR   Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR   PharmGKB; PA34934; -.
DR   VEuPathDB; HostDB:ENSG00000165821; -.
DR   eggNOG; KOG1074; Eukaryota.
DR   GeneTree; ENSGT00940000162245; -.
DR   HOGENOM; CLU_013111_0_0_1; -.
DR   InParanoid; Q9Y467; -.
DR   OrthoDB; 2880677at2759; -.
DR   PhylomeDB; Q9Y467; -.
DR   TreeFam; TF317003; -.
DR   PathwayCommons; Q9Y467; -.
DR   SignaLink; Q9Y467; -.
DR   SIGNOR; Q9Y467; -.
DR   BioGRID-ORCS; 6297; 12 hits in 1175 CRISPR screens.
DR   ChiTaRS; SALL2; human.
DR   GeneWiki; SALL2; -.
DR   GenomeRNAi; 6297; -.
DR   Pharos; Q9Y467; Tbio.
DR   PRO; PR:Q9Y467; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9Y467; Protein.
DR   Bgee; ENSG00000165821; Expressed in cerebellar vermis and 177 other cell types or tissues.
DR   ExpressionAtlas; Q9Y467; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0001654; P:eye development; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd20908; SUF4-like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23233; SAL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR23233:SF15; SAL-LIKE PROTEIN 2; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF13912; zf-C2H2_6; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
DR   Genevisible; Q9Y467; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1007
FT                   /note="Sal-like protein 2"
FT                   /id="PRO_0000047022"
FT   ZN_FING         34..56
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT                   ECO:0000303|PubMed:16545361"
FT   ZN_FING         373..395
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         401..423
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         631..653
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         659..681
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         691..713
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         911..933
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         940..963
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..174
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..780
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         797
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         802
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:21406692"
FT   CROSSLNK        911
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18655026"
FT   VAR_SEQ         1..24
FT                   /note="MSRRKQRKPQQLISDCEGPSASEN -> MAHESERSSRLGVPCGEPAELG
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056251"
FT   VAR_SEQ         131..200
FT                   /note="GTAAGGGGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHLNIPLI
FT                   LEELRVLQQRQIHQMQMT -> EPVCGIPVKWPAHEALEFQLHLHYHSKPGPTSAVWPR
FT                   NCGWEGASNNGIQGSQGEDSPPPISASCTQGSA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056252"
FT   VAR_SEQ         201..1007
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056253"
FT   VARIANT         75
FT                   /note="S -> C (in dbSNP:rs2242527)"
FT                   /id="VAR_014129"
FT   VARIANT         122
FT                   /note="S -> P (in dbSNP:rs1263811)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_014130"
FT   VARIANT         746
FT                   /note="R -> G (in dbSNP:rs1263810)"
FT                   /evidence="ECO:0000269|PubMed:9205841, ECO:0000269|Ref.6"
FT                   /id="VAR_014131"
FT   CONFLICT        547
FT                   /note="R -> L (in Ref. 1; X98834 and 5; AAI36529/AAI36530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="V -> M (in Ref. 1; X98834)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575..581
FT                   /note="FPYVLEP -> LPLCARA (in Ref. 1; X98834)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1007 AA;  105399 MW;  24B7C4ADE852B96C CRC64;
     MSRRKQRKPQ QLISDCEGPS ASENGDASEE DHPQVCAKCC AQFTDPTEFL AHQNACSTDP
     PVMVIIGGQE NPNNSSASSE PRPEGHNNPQ VMDTEHSNPP DSGSSVPTDP TWGPERRGEE
     SSGHFLVAAT GTAAGGGGGL ILASPKLGAT PLPPESTPAP PPPPPPPPPP GVGSGHLNIP
     LILEELRVLQ QRQIHQMQMT EQICRQVLLL GSLGQTVGAP ASPSELPGTG TASSTKPLLP
     LFSPIKPVQT SKTLASSSSS SSSSSGAETP KQAFFHLYHP LGSQHPFSAG GVGRSHKPTP
     APSPALPGST DQLIASPHLA FPSTTGLLAA QCLGAARGLE ATASPGLLKP KNGSGELSYG
     EVMGPLEKPG GRHKCRFCAK VFGSDSALQI HLRSHTGERP YKCNVCGNRF TTRGNLKVHF
     HRHREKYPHV QMNPHPVPEH LDYVITSSGL PYGMSVPPEK AEEEAATPGG GVERKPLVAS
     TTALSATESL TLLSTSAGTA TAPGLPAFNK FVLMKAVEPK NKADENTPPG SEGSAISGVA
     ESSTATRMQL SKLVTSLPSW ALLTNHFKST GSFPFPYVLE PLGASPSETS KLQQLVEKID
     RQGAVAVTSA ASGAPTTSAP APSSSASSGP NQCVICLRVL SCPRALRLHY GQHGGERPFK
     CKVCGRAFST RGNLRAHFVG HKASPAARAQ NSCPICQKKF TNAVTLQQHV RMHLGGQIPN
     GGTALPEGGG AAQENGSEQS TVSGARSFPQ QQSQQPSPEE ELSEEEEEED EEEEEDVTDE
     DSLAGRGSES GGEKAISVRG DSEEASGAEE EVGTVAAAAT AGKEMDSNEK TTQQSSLPPP
     PPPDSLDQPQ PMEQGSSGVL GGKEEGGKPE RSSSPASALT PEGEATSVTL VEELSLQEAM
     RKEPGESSSR KACEVCGQAF PSQAALEEHQ KTHPKEGPLF TCVFCRQGFL ERATLKKHML
     LAHHQVQPFA PHGPQNIAAL SLVPGCSPSI TSTGLSPFPR KDDPTIP
//