LOCUS       NP_612379                493 aa            linear   PRI 13-MAY-2024
DEFINITION  extracellular tyrosine-protein kinase PKDCC precursor [Homo
            sapiens].
ACCESSION   NP_612379 XP_038576
VERSION     NP_612379.2
DBSOURCE    REFSEQ: accession NM_138370.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Jung,J. and Wu,Q.
  TITLE     Identification of bone mineral density associated genes with shared
            genetic architectures across multiple tissues: Functional insights
            for EPDR1, PKDCC, and SPTBN1
  JOURNAL   PLoS One 19 (4), e0300535 (2024)
   PUBMED   38683846
  REMARK    GeneRIF: Identification of bone mineral density associated genes
            with shared genetic architectures across multiple tissues:
            Functional insights for EPDR1, PKDCC, and SPTBN1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Mohammed,J., Arora,N., Matthews,H.S., Hansen,K., Bader,M.,
            Walsh,S., Shaffer,J.R., Weinberg,S.M., Swigut,T., Claes,P.,
            Selleri,L. and Wysocka,J.
  TITLE     A common cis-regulatory variant impacts normal-range and
            disease-associated human facial shape through regulation of PKDCC
            during chondrogenesis
  JOURNAL   Elife 13, e82564 (2024)
   PUBMED   38483448
  REMARK    GeneRIF: A common cis-regulatory variant impacts normal-range and
            disease-associated human facial shape through regulation of PKDCC
            during chondrogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Yan,L., Cao,J., Zhang,Y., Liu,Y., Zou,J., Lou,B., Zhuang,D. and
            Li,H.
  TITLE     Prenatal diagnosis to identify compound heterozygous variants in
            PKDCC that causes rhizomelic limb shortening with dysmorphic
            features in a fetus from China
  JOURNAL   BMC Med Genomics 16 (1), 190 (2023)
   PUBMED   37592254
  REMARK    GeneRIF: Prenatal diagnosis to identify compound heterozygous
            variants in PKDCC that causes rhizomelic limb shortening with
            dysmorphic features in a fetus from China.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Pagnamenta,A.T., Belles,R.S., Salbert,B.A., Wentzensen,I.M.,
            Guillen Sacoto,M.J., Santos,F.J.R., Caffo,A., Ferla,M.,
            Banos-Pinero,B., Pawliczak,K., Makvand,M., Najmabadi,H.,
            Maroofian,R., Lester,T., Yanez-Felix,A.L., Villarroel-Cortes,C.E.,
            Xia,F., Al Fayez,K., Al Hashem,A., Shears,D., Irving,M.,
            Offiah,A.C., Kariminejad,A. and Taylor,J.C.
  CONSRTM   Genomics England Research Consortium
  TITLE     The prevalence and phenotypic range associated with biallelic PKDCC
            variants
  JOURNAL   Clin Genet 104 (1), 121-126 (2023)
   PUBMED   36896672
  REMARK    GeneRIF: The prevalence and phenotypic range associated with
            biallelic PKDCC variants.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Revollo,L., Merrill-Skoloff,G., De Ceunynck,K., Dilks,J.R., Guo,S.,
            Bordoli,M.R., Peters,C.G., Noetzli,L., Ionescu,A., Rosen,V.,
            Italiano,J.E., Whitman,M. and Flaumenhaft,R.
  TITLE     The secreted tyrosine kinase VLK is essential for normal platelet
            activation and thrombus formation
  JOURNAL   Blood 139 (1), 104-117 (2022)
   PUBMED   34329392
  REMARK    GeneRIF: The secreted tyrosine kinase VLK is essential for normal
            platelet activation and thrombus formation.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Castro-Giner,F., Bustamante,M., Ramon Gonzalez,J., Kogevinas,M.,
            Jarvis,D., Heinrich,J., Anto,J.M., Wjst,M., Estivill,X. and de
            Cid,R.
  TITLE     A pooling-based genome-wide analysis identifies new potential
            candidate genes for atopy in the European Community Respiratory
            Health Survey (ECRHS)
  JOURNAL   BMC Med Genet 10, 128 (2009)
   PUBMED   19961619
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Kinoshita,M., Era,T., Jakt,L.M. and Nishikawa,S.
  TITLE     The novel protein kinase Vlk is essential for stromal function of
            mesenchymal cells
  JOURNAL   Development 136 (12), 2069-2079 (2009)
   PUBMED   19465597
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Imuta,Y., Nishioka,N., Kiyonari,H. and Sasaki,H.
  TITLE     Short limbs, cleft palate, and delayed formation of flat
            proliferative chondrocytes in mice with targeted disruption of a
            putative protein kinase gene, Pkdcc (AW548124)
  JOURNAL   Dev Dyn 238 (1), 210-222 (2009)
   PUBMED   19097194
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB231841.1, DB457034.1, BM738316.1, AC013480.12, CF131963.1,
            BC110513.1 and BC062988.1.
            
            On Oct 3, 2008 this sequence version replaced NP_612379.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094697.1, ERR279870.3053.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294964.6/ ENSP00000294964.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..493
                     /product="extracellular tyrosine-protein kinase PKDCC
                     precursor"
                     /EC_number="2.7.10.2"
                     /note="vertebrate lonesome kinase; sugen kinase 493;
                     protein kinase domain-containing protein, cytoplasmic;
                     protein kinase-like protein SgK493; protein kinase domain
                     containing, cytoplasmic homolog; extracellular
                     tyrosine-protein kinase PKDCC"
                     /calculated_mol_wt=50785
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
                     /calculated_mol_wt=3365
     Region          28..128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q504Y2.2)"
     mat_peptide     33..493
                     /product="Extracellular tyrosine-protein kinase PKDCC.
                     /id=PRO_0000263010"
                     /note="propagated from UniProtKB/Swiss-Prot (Q504Y2.2)"
                     /calculated_mol_wt=50785
     Site            137
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Region          145..>295
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(145..147,150,152,164,166,212,233..236,278,282..283,
                     285,294..295)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5RJI4; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RJI4; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Site            320
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Site            369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Site            400
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Site            460
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     Site            484
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q504Y2.2)"
     CDS             1..493
                     /gene="PKDCC"
                     /gene_synonym="RLSDF; SGK493; Vlk"
                     /coded_by="NM_138370.3:180..1661"
                     /db_xref="CCDS:CCDS33186.2"
                     /db_xref="GeneID:91461"
                     /db_xref="HGNC:HGNC:25123"
                     /db_xref="MIM:614150"
ORIGIN      
        1 mrrrraavaa gfcasfllgs vlnvlfapgs epprpgqspe pspapgpgrr ggrgelarqi
       61 raryeevqry srggpgpgag rperrrlmdl apggpglprp rppwarplsd gapgwppapg
      121 pgspgpgprl gcaalrnvsg aqymgsgytk avyrvrlpgg aavalkavdf sghdlgscvr
      181 efgvrrgcyr laahkllkem vllerlrhpn vlqlygycyq dsedipdtlt titelgapve
      241 miqllqtswe drfriclslg rllhhlahsp lgsvtlldfr prqfvlvdge lkvtdlddar
      301 veetpcagst dcilefparn ftlpcsaqgw cegmnekrnl ynayrfffty llphsappsl
      361 rplldsivna tgelawgvde tlaqlekvlh lyrsgqylqn stasssteyq cipdstipqe
      421 dyrcwpsyhh gscllsvfnl aeavdvcesh aqcrafvvtn qttwtgrqlv ffktgwsqvv
      481 pdpnkttyvk asg
//
