GCP2_HUMAN
ID GCP2_HUMAN Reviewed; 902 AA.
AC Q9BSJ2; B4DM18; B7ZKL8; F5H4E0; F5H4L0; O43632; Q5VWX7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Gamma-tubulin complex component 2;
DE Short=GCP-2;
DE Short=hGCP2;
DE AltName: Full=Gamma-ring complex protein 103 kDa;
DE Short=h103p;
DE Short=hGrip103;
DE AltName: Full=Spindle pole body protein Spc97 homolog;
DE Short=hSpc97;
GN Name=TUBGCP2; Synonyms=GCP2;
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), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9566967; DOI=10.1083/jcb.141.3.663;
RA Murphy S.M., Urbani L., Stearns T.;
RT "The mammalian gamma-tubulin complex contains homologues of the yeast
RT spindle pole body components spc97p and spc98p.";
RL J. Cell Biol. 141:663-674(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Pancreas;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH ATF5.
RX PubMed=26213385; DOI=10.1016/j.cell.2015.06.055;
RA Madarampalli B., Yuan Y., Liu D., Lengel K., Xu Y., Li G., Yang J., Liu X.,
RA Lu Z., Liu D.X.;
RT "ATF5 Connects the Pericentriolar Materials to the Proximal End of the
RT Mother Centriole.";
RL Cell 162:580-592(2015).
RN [10]
RP INVOLVEMENT IN PAMDDFS, VARIANTS PAMDDFS CYS-297; CYS-333 AND PRO-615, AND
RP FUNCTION.
RX PubMed=31630790; DOI=10.1016/j.ajhg.2019.09.017;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA Mitani T., Punetha J., Akalin I., Pehlivan D., Dawidziuk M.,
RA Coban Akdemir Z., Yilmaz S., Aslan E., Hunter J.V., Hijazi H.,
RA Grochowski C.M., Jhangiani S.N., Karaca E., Fatih J.M., Iwanowski P.,
RA Gambin T., Wlasienko P., Goszczanska-Ciuchta A., Bekiesinska-Figatowska M.,
RA Hosseini M., Arzhangi S., Najmabadi H., Rosenfeld J.A., Du H., Marafi D.,
RA Blaser S., Teitelbaum R., Silver R., Posey J.E., Ropers H.H., Gibbs R.A.,
RA Wiszniewski W., Lupski J.R., Chitayat D., Kahrizi K., Gawlinski P.;
RT "Bi-allelic pathogenic variants in TUBGCP2 cause microcephaly and
RT lissencephaly spectrum disorders.";
RL Am. J. Hum. Genet. 105:1005-1015(2019).
CC -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation
CC at the centrosome. Plays a role in neuronal migration.
CC {ECO:0000269|PubMed:31630790, ECO:0000269|PubMed:9566967}.
CC -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2,
CC TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. Interacts with ATF5; the
CC ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite unites the mother
CC centriole and the pericentriolar material (PCM) in the centrosome
CC (PubMed:26213385). {ECO:0000269|PubMed:26213385,
CC ECO:0000269|PubMed:9566967}.
CC -!- INTERACTION:
CC Q9BSJ2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-357881, EBI-748621;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:9566967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms may exist. May be produced at very low
CC levels due to a premature stop codon in the mRNA, leading to
CC nonsense-mediated mRNA decay.;
CC Name=1;
CC IsoId=Q9BSJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BSJ2-3; Sequence=VSP_044698;
CC Name=3;
CC IsoId=Q9BSJ2-4; Sequence=VSP_045982;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DISEASE: Pachygyria, microcephaly, developmental delay, and dysmorphic
CC facies, with or without seizures (PAMDDFS) [MIM:618737]: An autosomal
CC recessive disorder characterized by global developmental delay,
CC variably impaired intellectual development, speech delay, facial
CC dysmorphism, microcephaly, and varying degrees of cortical
CC malformations including pachygyria, thin corpus callosum and
CC subcortical band heterotopia. Most patients have generalized seizures.
CC {ECO:0000269|PubMed:31630790}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC005011; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF042379; AAC39728.1; -; mRNA.
DR EMBL; AK297251; BAG59730.1; -; mRNA.
DR EMBL; AL360181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005011; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC093770; AAH93770.1; -; mRNA.
DR EMBL; BC111957; AAI11958.1; -; mRNA.
DR EMBL; BC143247; AAI43248.1; -; mRNA.
DR CCDS; CCDS58104.1; -. [Q9BSJ2-3]
DR CCDS; CCDS58105.1; -. [Q9BSJ2-4]
DR CCDS; CCDS7676.1; -. [Q9BSJ2-1]
DR RefSeq; NP_001243546.1; NM_001256617.1. [Q9BSJ2-4]
DR RefSeq; NP_001243547.1; NM_001256618.1. [Q9BSJ2-3]
DR RefSeq; NP_006650.1; NM_006659.3. [Q9BSJ2-1]
DR PDB; 6V6B; EM; 3.80 A; C=1-902.
DR PDB; 6V6S; EM; 4.30 A; A/C/E/G/M=1-902.
DR PDB; 6X0V; EM; 4.50 A; F=1-902.
DR PDB; 7AS4; EM; 4.13 A; A/C/E/G/M=1-902.
DR PDB; 7QJ0; EM; 5.32 A; G=1-902.
DR PDB; 7QJ1; EM; 7.00 A; G=1-902.
DR PDB; 7QJ2; EM; 8.60 A; E/G=1-902.
DR PDB; 7QJ3; EM; 7.60 A; G/M=1-902.
DR PDB; 7QJ4; EM; 9.00 A; E/G/M=1-902.
DR PDB; 7QJ5; EM; 8.70 A; A/C/E/G/M=1-902.
DR PDB; 7QJ6; EM; 7.80 A; C/E/G=1-902.
DR PDB; 7QJ7; EM; 8.70 A; A/C/E/G=1-902.
DR PDB; 7QJ8; EM; 8.70 A; C/E/G/M=1-902.
DR PDB; 7QJ9; EM; 8.10 A; C/E/G=1-902.
DR PDB; 7QJA; EM; 9.20 A; A/C/E/G=1-902.
DR PDB; 7QJB; EM; 9.20 A; C/E/G/M=1-902.
DR PDB; 7QJC; EM; 16.10 A; A/C/E/G/M=1-902.
DR PDB; 7QJD; EM; 7.10 A; A/C/E/G/M=1-902.
DR PDBsum; 6V6B; -.
DR PDBsum; 6V6S; -.
DR PDBsum; 6X0V; -.
DR PDBsum; 7AS4; -.
DR PDBsum; 7QJ0; -.
DR PDBsum; 7QJ1; -.
DR PDBsum; 7QJ2; -.
DR PDBsum; 7QJ3; -.
DR PDBsum; 7QJ4; -.
DR PDBsum; 7QJ5; -.
DR PDBsum; 7QJ6; -.
DR PDBsum; 7QJ7; -.
DR PDBsum; 7QJ8; -.
DR PDBsum; 7QJ9; -.
DR PDBsum; 7QJA; -.
DR PDBsum; 7QJB; -.
DR PDBsum; 7QJC; -.
DR PDBsum; 7QJD; -.
DR AlphaFoldDB; Q9BSJ2; -.
DR SMR; Q9BSJ2; -.
DR BioGRID; 116055; 173.
DR CORUM; Q9BSJ2; -.
DR IntAct; Q9BSJ2; 73.
DR MINT; Q9BSJ2; -.
DR STRING; 9606.ENSP00000446093; -.
DR GlyGen; Q9BSJ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BSJ2; -.
DR MetOSite; Q9BSJ2; -.
DR PhosphoSitePlus; Q9BSJ2; -.
DR BioMuta; TUBGCP2; -.
DR DMDM; 21450889; -.
DR EPD; Q9BSJ2; -.
DR jPOST; Q9BSJ2; -.
DR MassIVE; Q9BSJ2; -.
DR MaxQB; Q9BSJ2; -.
DR PaxDb; Q9BSJ2; -.
DR PeptideAtlas; Q9BSJ2; -.
DR PRIDE; Q9BSJ2; -.
DR ProteomicsDB; 26543; -.
DR ProteomicsDB; 26604; -.
DR ProteomicsDB; 78900; -. [Q9BSJ2-1]
DR Antibodypedia; 46457; 176 antibodies from 29 providers.
DR DNASU; 10844; -.
DR Ensembl; ENST00000252936.8; ENSP00000252936.3; ENSG00000130640.15. [Q9BSJ2-1]
DR Ensembl; ENST00000417178.7; ENSP00000395666.2; ENSG00000130640.15. [Q9BSJ2-3]
DR Ensembl; ENST00000543663.6; ENSP00000446093.1; ENSG00000130640.15. [Q9BSJ2-4]
DR Ensembl; ENST00000682123.1; ENSP00000507610.1; ENSG00000130640.15. [Q9BSJ2-1]
DR Ensembl; ENST00000682515.1; ENSP00000506731.1; ENSG00000130640.15. [Q9BSJ2-1]
DR Ensembl; ENST00000683612.1; ENSP00000507482.1; ENSG00000130640.15. [Q9BSJ2-1]
DR GeneID; 10844; -.
DR KEGG; hsa:10844; -.
DR MANE-Select; ENST00000252936.8; ENSP00000252936.3; NM_006659.4; NP_006650.1.
DR UCSC; uc001lmg.2; human. [Q9BSJ2-1]
DR CTD; 10844; -.
DR DisGeNET; 10844; -.
DR GeneCards; TUBGCP2; -.
DR HGNC; HGNC:18599; TUBGCP2.
DR HPA; ENSG00000130640; Low tissue specificity.
DR MalaCards; TUBGCP2; -.
DR MIM; 617817; gene.
DR MIM; 618737; phenotype.
DR neXtProt; NX_Q9BSJ2; -.
DR OpenTargets; ENSG00000130640; -.
DR PharmGKB; PA38598; -.
DR VEuPathDB; HostDB:ENSG00000130640; -.
DR eggNOG; KOG2001; Eukaryota.
DR GeneTree; ENSGT00940000156697; -.
DR InParanoid; Q9BSJ2; -.
DR OMA; SKLMTCC; -.
DR OrthoDB; 679187at2759; -.
DR PhylomeDB; Q9BSJ2; -.
DR TreeFam; TF324047; -.
DR PathwayCommons; Q9BSJ2; -.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR SignaLink; Q9BSJ2; -.
DR SIGNOR; Q9BSJ2; -.
DR BioGRID-ORCS; 10844; 705 hits in 1088 CRISPR screens.
DR ChiTaRS; TUBGCP2; human.
DR GeneWiki; TUBGCP2; -.
DR GenomeRNAi; 10844; -.
DR Pharos; Q9BSJ2; Tbio.
DR PRO; PR:Q9BSJ2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BSJ2; protein.
DR Bgee; ENSG00000130640; Expressed in right uterine tube and 193 other tissues.
DR ExpressionAtlas; Q9BSJ2; baseline and differential.
DR Genevisible; Q9BSJ2; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0008275; C:gamma-tubulin small complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Epilepsy; Intellectual disability; Lissencephaly;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..902
FT /note="Gamma-tubulin complex component 2"
FT /id="PRO_0000078113"
FT REGION 874..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044698"
FT VAR_SEQ 205
FT /note="I -> IVLLRWNLALSPRLKCSGVISAHCNLHLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045982"
FT VARIANT 111
FT /note="A -> T (in dbSNP:rs2298121)"
FT /id="VAR_022126"
FT VARIANT 193
FT /note="I -> T (in dbSNP:rs11101682)"
FT /id="VAR_049249"
FT VARIANT 297
FT /note="R -> C (in PAMDDFS; unknown pathological
FT significance; dbSNP:rs200129338)"
FT /evidence="ECO:0000269|PubMed:31630790"
FT /id="VAR_083747"
FT VARIANT 333
FT /note="R -> C (in PAMDDFS; unknown pathological
FT significance; dbSNP:rs34832477)"
FT /evidence="ECO:0000269|PubMed:31630790"
FT /id="VAR_083748"
FT VARIANT 615
FT /note="A -> P (in PAMDDFS; unknown pathological
FT significance; dbSNP:rs1449999247)"
FT /evidence="ECO:0000269|PubMed:31630790"
FT /id="VAR_083749"
FT VARIANT 809
FT /note="A -> T (in dbSNP:rs11101677)"
FT /id="VAR_049250"
FT CONFLICT 279
FT /note="E -> G (in Ref. 2; BAG59730)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="L -> F (in Ref. 4; BC005011)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9BSJ2-4:209
FT /note="R -> G (in Ref. 4; AAI43248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 902 AA; 102534 MW; 4FAAF864A3758E6A CRC64;
MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP
EDFLKKYDEL KSKNTRNLDP LVYLLSKLTE DKETLQYLQQ NAKERAELAA AAVGSSTTSI
NVPAAASKIS MQELEELRKQ LGSVATGSTL QQSLELKRKM LRDKQNKKNS GQHLPIFPAW
VYERPALIGD FLIGAGISTD TALPIGTLPL ASQESAVVED LLYVLVGVDG RYVSAQPLAG
RQSRTFLVDP NLDLSIRELV HRILPVAASY SAVTRFIEEK SSFEYGQVNH ALAAAMRTLV
KEHLILVSQL EQLHRQGLLS LQKLWFYIQP AMRTMDILAS LATSVDKGEC LGGSTLSLLH
DRSFSYTGDS QAQELCLYLT KAASAPYFEV LEKWIYRGII HDPYSEFMVE EHELRKERIQ
EDYNDKYWDQ RYTIVQQQIP SFLQKMADKI LSTGKYLNVV RECGHDVTCP VAKEIIYTLK
ERAYVEQIEK AFNYASKVLL DFLMEEKELV AHLRSIKRYF LMDQGDFFVH FMDLAEEELR
KPVEDITPPR LEALLELALR MSTANTDPFK DDLKIDLMPH DLITQLLRVL AIETKQEKAM
AHADPTELAL SGLEAFSFDY IVKWPLSLII NRKALTRYQM LFRHMFYCKH VERQLCSVWI
SNKTAKQHSL HSAQWFAGAF TLRQRMLNFV QNIQYYMMFE VMEPTWHILE KNLKSASNID
DVLGHHTGFL DTCLKDCMLT NPELLKVFSK LMSVCVMFTN CMQKFTQSMK LDGELGGQTL
EHSTVLGLPA GAEERARKEL ARKHLAEHAD TVQLVSGFEA TINKFDKNFS AHLLDLLARL
SIYSTSDCEH GMASVISRLD FNGFYTERLE RLSAERSQKA TPQVPVLRGP PAPAPRVAVT
AQ
