GLT12_HUMAN
ID GLT12_HUMAN Reviewed; 581 AA.
AC Q8IXK2; Q5TCF7; Q8NG54; Q96CT9; Q9H771;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 12;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 12;
DE Short=GalNAc-T12;
DE Short=pp-GaNTase 12;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 12;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12;
GN Name=GALNT12;
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), ENZYME ACTIVITY, TISSUE
RP SPECIFICITY, AND VARIANT VAL-119.
RC TISSUE=Lung;
RX PubMed=12135769; DOI=10.1016/s0014-5793(02)03007-7;
RA Guo J.-M., Zhang Y., Cheng L., Iwasaki H., Wang H., Kubota T.,
RA Tachibana K., Narimatsu H.;
RT "Molecular cloning and characterization of a novel member of the UDP-
RT GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-
RT T12(1).";
RL FEBS Lett. 524:211-218(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bennett E.P.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
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 [LARGE SCALE MRNA] OF 144-581 (ISOFORM 1).
RC TISSUE=Colon;
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 [6]
RP VARIANTS CRCS1 TRP-297; ASN-303; ASP-341; HIS-373; HIS-382; PHE-479 AND
RP MET-491, CHARACTERIZATION OF VARIANTS CRCS1 TRP-297; ASN-303; ASP-341;
RP HIS-373; HIS-382; PHE-479 AND MET-491, AND VARIANTS GLU-3; ARG-46; VAL-119;
RP ASN-261; ARG-272 AND LYS-552.
RX PubMed=19617566; DOI=10.1073/pnas.0901454106;
RA Guda K., Moinova H., He J., Jamison O., Ravi L., Natale L., Lutterbaugh J.,
RA Lawrence E., Lewis S., Willson J.K., Lowe J.B., Wiesner G.L.,
RA Parmigiani G., Barnholtz-Sloan J., Dawson D.W., Velculescu V.E.,
RA Kinzler K.W., Papadopoulos N., Vogelstein B., Willis J., Gerken T.A.,
RA Markowitz S.D.;
RT "Inactivating germ-line and somatic mutations in polypeptide N-
RT acetylgalactosaminyltransferase 12 in human colon cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12921-12925(2009).
RN [7]
RP VARIANTS CRCS1 ASN-303 AND CYS-396.
RX PubMed=22461326; DOI=10.1002/humu.22088;
RA Clarke E., Green R.C., Green J.S., Mahoney K., Parfrey P.S.,
RA Younghusband H.B., Woods M.O.;
RT "Inherited deleterious variants in GALNT12 are associated with CRC
RT susceptibility.";
RL Hum. Mutat. 33:1056-1058(2012).
RN [8]
RP INVOLVEMENT IN CRCS1.
RX PubMed=24115450; DOI=10.1002/humu.22454;
RA Segui N., Pineda M., Navarro M., Lazaro C., Brunet J., Infante M.,
RA Duran M., Soto J.L., Blanco I., Capella G., Valle L.;
RT "GALNT12 is not a major contributor of familial colorectal cancer type X.";
RL Hum. Mutat. 35:50-52(2014).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has activity
CC toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no
CC detectable activity with Muc2 and Muc7. Displays enzymatic activity
CC toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to
CC mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an
CC important role in the initial step of mucin-type oligosaccharide
CC biosynthesis in digestive organs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:12135769};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:12135769};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IXK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXK2-2; Sequence=VSP_011217;
CC -!- TISSUE SPECIFICITY: Widely expressed at different levels of expression.
CC Highly expressed in digestive organs such as small intestine, stomach,
CC pancreas and colon. Expressed at intermediate level in testis, thyroid
CC gland and spleen. Weakly expressed in whole brain, cerebral cortex,
CC cerebellum, fetal brain, bone marrow, thymus, leukocytes, heart,
CC skeletal muscle, liver, lung, esophagus, kidney, adrenal gland, mammary
CC gland, uterus, placenta, ovary and prostate.
CC {ECO:0000269|PubMed:12135769}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- DISEASE: Colorectal cancer 1 (CRCS1) [MIM:608812]: A complex disease
CC characterized by malignant lesions arising from the inner wall of the
CC large intestine (the colon) and the rectum. Genetic alterations are
CC often associated with progression from premalignant lesion (adenoma) to
CC invasive adenocarcinoma. Risk factors for cancer of the colon and
CC rectum include colon polyps, long-standing ulcerative colitis, and
CC genetic family history. {ECO:0000269|PubMed:19617566,
CC ECO:0000269|PubMed:22461326, ECO:0000269|PubMed:24115450}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry. The role of GALNT12 in colon cancer
CC susceptibility is however subject to discussion: studies on 103
CC probants with colorectal cancer 1 (CRCS1) suggest that it does not act
CC as a major contributor of CRCS1 (PubMed:24115450).
CC {ECO:0000269|PubMed:24115450}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 12;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_495";
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DR EMBL; AB078146; BAC07181.1; -; mRNA.
DR EMBL; AJ132365; CAC80100.2; -; mRNA.
DR EMBL; AL136084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013945; AAH13945.1; -; mRNA.
DR EMBL; AK024865; BAB15027.1; ALT_INIT; mRNA.
DR CCDS; CCDS6737.1; -. [Q8IXK2-1]
DR RefSeq; NP_078918.3; NM_024642.4. [Q8IXK2-1]
DR RefSeq; XP_006717350.1; XM_006717287.1.
DR PDB; 6PXU; X-ray; 2.01 A; A/B=39-581.
DR PDBsum; 6PXU; -.
DR AlphaFoldDB; Q8IXK2; -.
DR SMR; Q8IXK2; -.
DR BioGRID; 122816; 118.
DR IntAct; Q8IXK2; 33.
DR MINT; Q8IXK2; -.
DR STRING; 9606.ENSP00000364150; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR UniLectin; Q8IXK2; -.
DR iPTMnet; Q8IXK2; -.
DR PhosphoSitePlus; Q8IXK2; -.
DR SwissPalm; Q8IXK2; -.
DR BioMuta; GALNT12; -.
DR DMDM; 84028209; -.
DR EPD; Q8IXK2; -.
DR jPOST; Q8IXK2; -.
DR MassIVE; Q8IXK2; -.
DR MaxQB; Q8IXK2; -.
DR PaxDb; Q8IXK2; -.
DR PeptideAtlas; Q8IXK2; -.
DR PRIDE; Q8IXK2; -.
DR ProteomicsDB; 71019; -. [Q8IXK2-1]
DR ProteomicsDB; 71020; -. [Q8IXK2-2]
DR Antibodypedia; 29005; 90 antibodies from 15 providers.
DR DNASU; 79695; -.
DR Ensembl; ENST00000375011.4; ENSP00000364150.3; ENSG00000119514.7. [Q8IXK2-1]
DR GeneID; 79695; -.
DR KEGG; hsa:79695; -.
DR MANE-Select; ENST00000375011.4; ENSP00000364150.3; NM_024642.5; NP_078918.3.
DR UCSC; uc004ayz.3; human. [Q8IXK2-1]
DR CTD; 79695; -.
DR DisGeNET; 79695; -.
DR GeneCards; GALNT12; -.
DR HGNC; HGNC:19877; GALNT12.
DR HPA; ENSG00000119514; Tissue enhanced (epididymis, intestine, stomach).
DR MalaCards; GALNT12; -.
DR MIM; 608812; phenotype.
DR MIM; 610290; gene.
DR neXtProt; NX_Q8IXK2; -.
DR OpenTargets; ENSG00000119514; -.
DR PharmGKB; PA134929192; -.
DR VEuPathDB; HostDB:ENSG00000119514; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000157173; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; Q8IXK2; -.
DR OMA; QFNWHAV; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8IXK2; -.
DR TreeFam; TF352660; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q8IXK2; -.
DR Reactome; R-HSA-5083636; Defective GALNT12 causes CRCS1.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q8IXK2; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 79695; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; GALNT12; human.
DR GenomeRNAi; 79695; -.
DR Pharos; Q8IXK2; Tbio.
DR PRO; PR:Q8IXK2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IXK2; protein.
DR Bgee; ENSG00000119514; Expressed in palpebral conjunctiva and 151 other tissues.
DR ExpressionAtlas; Q8IXK2; baseline and differential.
DR Genevisible; Q8IXK2; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Polypeptide N-acetylgalactosaminyltransferase 12"
FT /id="PRO_0000059128"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..581
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 445..577
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 43..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..244
FT /note="Catalytic subdomain A"
FT REGION 304..366
FT /note="Catalytic subdomain B"
FT COMPBIAS 51..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 125..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 349..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 458..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 506..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 547..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 1..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011217"
FT VARIANT 3
FT /note="G -> E (in dbSNP:rs1356894484)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064352"
FT VARIANT 46
FT /note="G -> R (in dbSNP:rs10987768)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064353"
FT VARIANT 119
FT /note="E -> V (in dbSNP:rs1137654)"
FT /evidence="ECO:0000269|PubMed:12135769,
FT ECO:0000269|PubMed:19617566"
FT /id="VAR_064354"
FT VARIANT 261
FT /note="D -> N (in dbSNP:rs41306504)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064355"
FT VARIANT 272
FT /note="G -> R (in dbSNP:rs367645298)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064356"
FT VARIANT 297
FT /note="R -> W (in CRCS1; germline mutation; partial loss of
FT activity; dbSNP:rs149726976)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064357"
FT VARIANT 303
FT /note="D -> N (in CRCS1; germline mutation; reduction of
FT activity; dbSNP:rs145236923)"
FT /evidence="ECO:0000269|PubMed:19617566,
FT ECO:0000269|PubMed:22461326"
FT /id="VAR_064358"
FT VARIANT 341
FT /note="E -> D (in CRCS1; somatic mutation; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064359"
FT VARIANT 373
FT /note="R -> H (in CRCS1; germline mutation; partial loss of
FT activity; dbSNP:rs920049418)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064360"
FT VARIANT 382
FT /note="R -> H (in CRCS1; germline mutation; loss of
FT activity; dbSNP:rs868590153)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064361"
FT VARIANT 396
FT /note="Y -> C (in CRCS1; dbSNP:rs1272530441)"
FT /evidence="ECO:0000269|PubMed:22461326"
FT /id="VAR_068509"
FT VARIANT 479
FT /note="C -> F (in CRCS1; somatic mutation; loss of
FT activity)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064362"
FT VARIANT 491
FT /note="T -> M (in CRCS1; germline mutation; loss of
FT activity; dbSNP:rs267606840)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064363"
FT VARIANT 552
FT /note="R -> K (in dbSNP:rs1285871027)"
FT /evidence="ECO:0000269|PubMed:19617566"
FT /id="VAR_064364"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6PXU"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:6PXU"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:6PXU"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 352..364
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 376..387
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 425..431
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 445..454
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:6PXU"
FT TURN 542..545
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:6PXU"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:6PXU"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:6PXU"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:6PXU"
SQ SEQUENCE 581 AA; 66938 MW; 8C001D58E103A523 CRC64;
MWGRTARRRC PRELRRGREA LLVLLALLAL AGLGSVLRAQ RGAGAGAAEP GPPRTPRPGR
REPVMPRPPV PANALGARGE AVRLQLQGEE LRLQEESVRL HQINIYLSDR ISLHRRLPER
WNPLCKEKKY DYDNLPRTSV IIAFYNEAWS TLLRTVYSVL ETSPDILLEE VILVDDYSDR
EHLKERLANE LSGLPKVRLI RANKREGLVR ARLLGASAAR GDVLTFLDCH CECHEGWLEP
LLQRIHEEES AVVCPVIDVI DWNTFEYLGN SGEPQIGGFD WRLVFTWHTV PERERIRMQS
PVDVIRSPTM AGGLFAVSKK YFEYLGSYDT GMEVWGGENL EFSFRIWQCG GVLETHPCSH
VGHVFPKQAP YSRNKALANS VRAAEVWMDE FKELYYHRNP RARLEPFGDV TERKQLRDKL
QCKDFKWFLE TVYPELHVPE DRPGFFGMLQ NKGLTDYCFD YNPPDENQIV GHQVILYLCH
GMGQNQFFEY TSQKEIRYNT HQPEGCIAVE AGMDTLIMHL CEETAPENQK FILQEDGSLF
HEQSKKCVQA ARKESSDSFV PLLRDCTNSD HQKWFFKERM L
