ID   CLH2_HUMAN              Reviewed;        1640 AA.
AC   P53675; B7Z7U5; Q14017; Q15808; Q15809;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Clathrin heavy chain 2;
DE   AltName: Full=Clathrin heavy chain on chromosome 22;
DE            Short=CLH-22;
GN   Name=CLTCL1; Synonyms=CLH22, CLTCL, CLTD;
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=Fetal brain;
RX   PubMed=8733128; DOI=10.1093/hmg/5.5.617;
RA   Sirotkin H., Morrow B., Dasgupta R., Goldberg R., Patangali S.R., Shi G.,
RA   Cannizzaro L., Shprintzen R., Weissman S., Kucherlapati R.;
RT   "Isolation of a new clathrin heavy chain gene with muscle-specific
RT   expression from the region commonly deleted in velo-cardio-facial
RT   syndrome.";
RL   Hum. Mol. Genet. 5:617-624(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP   1451-1640 (ISOFORM 2).
RC   TISSUE=Fetal brain, and Skeletal muscle;
RX   PubMed=8733129; DOI=10.1093/hmg/5.5.625;
RA   Kedra D., Peyrard M., Fransson I., Collins J.E., Dunham I., Roe B.A.,
RA   Dumanski J.P.;
RT   "Characterization of a second human clathrin heavy chain polypeptide gene
RT   (CLH-22) from chromosome 22q11.";
RL   Hum. Mol. Genet. 5:625-631(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT LYS-691.
RX   PubMed=8844170; DOI=10.1006/geno.1996.0386;
RA   Long K.R., Trofatter J.A., Ramesh V., McCormick M.K., Buckler A.J.;
RT   "Cloning and characterization of a novel human clathrin heavy chain gene
RT   (CLTCL).";
RL   Genomics 35:466-472(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH AFTPH.
RX   PubMed=15758025; DOI=10.1091/mbc.e04-12-1077;
RA   Hirst J., Borner G.H., Harbour M., Robinson M.S.;
RT   "The aftiphilin/p200/gamma-synergin complex.";
RL   Mol. Biol. Cell 16:2554-2565(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles. Two different adapter protein complexes link
CC       the clathrin lattice either to the plasma membrane or to the trans-
CC       Golgi network (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC       chains, are the basic subunits of the clathrin coat (By similarity). In
CC       the presence of light chains, hub assembly is influenced by both the pH
CC       and the concentration of calcium (Probable). May interact with OCRL (By
CC       similarity). Interacts with AFTPH/aftiphilin (PubMed:15758025).
CC       {ECO:0000250|UniProtKB:Q00610, ECO:0000250|UniProtKB:Q68FD5,
CC       ECO:0000269|PubMed:15758025, ECO:0000305}.
CC   -!- INTERACTION:
CC       P53675; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-358826, EBI-25475920;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic
CC       face of coated pits and vesicles. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long, Brain;
CC         IsoId=P53675-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, Muscle;
CC         IsoId=P53675-2; Sequence=VSP_001100;
CC   -!- TISSUE SPECIFICITY: Maximal levels in skeletal muscle. High levels in
CC       heart and testis. Low expression detected in all other tissues.
CC   -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of the
CC       triskelion. This region contains the trimerization domain and the
CC       light-chain binding domain involved in the assembly of the clathrin
CC       lattice.
CC   -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC       like repeats, and projects inward from the polyhedral outer clathrin
CC       coat. It constitutes a major protein-protein interaction node (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/361/CLTCL1";
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DR   EMBL; U41763; AAC50494.1; -; mRNA.
DR   EMBL; X95486; CAA64752.1; -; mRNA.
DR   EMBL; X95487; CAA64753.1; -; mRNA.
DR   EMBL; U60802; AAB40908.1; -; mRNA.
DR   EMBL; U60803; AAB40909.1; -; mRNA.
DR   EMBL; AK302506; BAH13731.1; -; mRNA.
DR   EMBL; CH471176; EAX03047.1; -; Genomic_DNA.
DR   CCDS; CCDS46662.2; -. [P53675-1]
DR   CCDS; CCDS54497.2; -. [P53675-2]
DR   PIR; G02757; G02757.
DR   PIR; T09522; T09522.
DR   RefSeq; NP_001826.3; NM_001835.3. [P53675-2]
DR   RefSeq; NP_009029.3; NM_007098.3. [P53675-1]
DR   AlphaFoldDB; P53675; -.
DR   SMR; P53675; -.
DR   BioGRID; 113854; 228.
DR   IntAct; P53675; 71.
DR   MINT; P53675; -.
DR   STRING; 9606.ENSP00000441158; -.
DR   MoonDB; P53675; Curated.
DR   TCDB; 8.A.137.1.2; the clathrin (clathrin) family.
DR   GlyGen; P53675; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P53675; -.
DR   MetOSite; P53675; -.
DR   PhosphoSitePlus; P53675; -.
DR   SwissPalm; P53675; -.
DR   BioMuta; CLTCL1; -.
DR   DMDM; 2506298; -.
DR   EPD; P53675; -.
DR   jPOST; P53675; -.
DR   MassIVE; P53675; -.
DR   MaxQB; P53675; -.
DR   PaxDb; 9606-ENSP00000441158; -.
DR   PeptideAtlas; P53675; -.
DR   ProteomicsDB; 56608; -. [P53675-1]
DR   ProteomicsDB; 56609; -. [P53675-2]
DR   Pumba; P53675; -.
DR   Antibodypedia; 50558; 139 antibodies from 21 providers.
DR   DNASU; 8218; -.
DR   Ensembl; ENST00000427926.6; ENSP00000441158.1; ENSG00000070371.16. [P53675-1]
DR   Ensembl; ENST00000621271.4; ENSP00000485020.1; ENSG00000070371.16. [P53675-2]
DR   GeneID; 8218; -.
DR   KEGG; hsa:8218; -.
DR   MANE-Select; ENST00000427926.6; ENSP00000441158.1; NM_007098.4; NP_009029.3.
DR   UCSC; uc032qgb.2; human. [P53675-1]
DR   AGR; HGNC:2093; -.
DR   CTD; 8218; -.
DR   DisGeNET; 8218; -.
DR   GeneCards; CLTCL1; -.
DR   GeneReviews; CLTCL1; -.
DR   HGNC; HGNC:2093; CLTCL1.
DR   HPA; ENSG00000070371; Group enriched (skeletal muscle, testis, tongue).
DR   MalaCards; CLTCL1; -.
DR   MIM; 601273; gene.
DR   neXtProt; NX_P53675; -.
DR   OpenTargets; ENSG00000070371; -.
DR   Orphanet; 453510; Congenital insensitivity to pain with severe intellectual disability.
DR   PharmGKB; PA26619; -.
DR   VEuPathDB; HostDB:ENSG00000070371; -.
DR   eggNOG; KOG0985; Eukaryota.
DR   GeneTree; ENSGT00950000183166; -.
DR   InParanoid; P53675; -.
DR   OMA; HTRVMDY; -.
DR   OrthoDB; 5474327at2759; -.
DR   PhylomeDB; P53675; -.
DR   TreeFam; TF300059; -.
DR   PathwayCommons; P53675; -.
DR   Reactome; R-HSA-190873; Gap junction degradation.
DR   Reactome; R-HSA-196025; Formation of annular gap junctions.
DR   Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   SignaLink; P53675; -.
DR   SIGNOR; P53675; -.
DR   BioGRID-ORCS; 8218; 29 hits in 1164 CRISPR screens.
DR   ChiTaRS; CLTCL1; human.
DR   GenomeRNAi; 8218; -.
DR   Pharos; P53675; Tbio.
DR   PRO; PR:P53675; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; P53675; Protein.
DR   Bgee; ENSG00000070371; Expressed in gastrocnemius and 133 other cell types or tissues.
DR   ExpressionAtlas; P53675; baseline and differential.
DR   GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR   GO; GO:0071439; C:clathrin complex; IBA:GO_Central.
DR   GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR   GO; GO:0030135; C:coated vesicle; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0097443; C:sorting endosome; IDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0046326; P:positive regulation of glucose import; IMP:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR   Gene3D; 1.25.40.730; -; 1.
DR   Gene3D; 2.130.10.110; Clathrin heavy-chain terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR   InterPro; IPR016025; Clathrin_H-chain_N.
DR   InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR   InterPro; IPR016341; Clathrin_heavy_chain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10292:SF6; CLATHRIN HEAVY CHAIN 2; 1.
DR   PANTHER; PTHR10292; CLATHRIN HEAVY CHAIN RELATED; 1.
DR   Pfam; PF00637; Clathrin; 7.
DR   Pfam; PF09268; Clathrin-link; 1.
DR   Pfam; PF13838; Clathrin_H_link; 1.
DR   Pfam; PF01394; Clathrin_propel; 5.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM repeat; 6.
DR   SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR   PROSITE; PS50236; CHCR; 7.
DR   Genevisible; P53675; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coated pit; Cytoplasmic vesicle;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   CHAIN           2..1640
FT                   /note="Clathrin heavy chain 2"
FT                   /id="PRO_0000205786"
FT   REPEAT          537..683
FT                   /note="CHCR 1"
FT   REPEAT          686..828
FT                   /note="CHCR 2"
FT   REPEAT          833..972
FT                   /note="CHCR 3"
FT   REPEAT          979..1124
FT                   /note="CHCR 4"
FT   REPEAT          1128..1269
FT                   /note="CHCR 5"
FT   REPEAT          1274..1420
FT                   /note="CHCR 6"
FT   REPEAT          1423..1566
FT                   /note="CHCR 7"
FT   REGION          2..479
FT                   /note="Globular terminal domain"
FT   REGION          24..67
FT                   /note="WD40-like repeat 1"
FT   REGION          68..107
FT                   /note="WD40-like repeat 2"
FT   REGION          108..149
FT                   /note="WD40-like repeat 3"
FT   REGION          150..195
FT                   /note="WD40-like repeat 4"
FT   REGION          196..257
FT                   /note="WD40-like repeat 5"
FT   REGION          258..301
FT                   /note="WD40-like repeat 6"
FT   REGION          302..330
FT                   /note="WD40-like repeat 7"
FT   REGION          449..465
FT                   /note="Binding site for the uncoating ATPase, involved in
FT                   lattice disassembly"
FT                   /evidence="ECO:0000255"
FT   REGION          480..523
FT                   /note="Flexible linker"
FT   REGION          524..1640
FT                   /note="Heavy chain arm"
FT   REGION          524..634
FT                   /note="Distal segment"
FT   REGION          639..1640
FT                   /note="Proximal segment"
FT   REGION          1213..1522
FT                   /note="Involved in binding clathrin light chain"
FT                   /evidence="ECO:0000250"
FT   REGION          1551..1640
FT                   /note="Trimerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         184
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         634
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         737
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         856
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         899
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         1167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         1206
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         1229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         1441
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         1441
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         1477
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         1487
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FD5"
FT   MOD_RES         1494
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   MOD_RES         1501
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00610"
FT   VAR_SEQ         1479..1535
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:8733129, ECO:0000303|PubMed:8844170"
FT                   /id="VSP_001100"
FT   VARIANT         61
FT                   /note="P -> L (in dbSNP:rs3747059)"
FT                   /id="VAR_055653"
FT   VARIANT         205
FT                   /note="K -> R (in dbSNP:rs5746697)"
FT                   /id="VAR_055654"
FT   VARIANT         279
FT                   /note="Y -> C (in dbSNP:rs807459)"
FT                   /id="VAR_055655"
FT   VARIANT         691
FT                   /note="E -> K (in dbSNP:rs1060374)"
FT                   /evidence="ECO:0000269|PubMed:8844170"
FT                   /id="VAR_055656"
FT   VARIANT         941
FT                   /note="K -> R (in dbSNP:rs35398725)"
FT                   /id="VAR_055657"
FT   VARIANT         945
FT                   /note="R -> H (in dbSNP:rs36077768)"
FT                   /id="VAR_055658"
FT   VARIANT         1046
FT                   /note="R -> C (in dbSNP:rs712952)"
FT                   /id="VAR_055659"
FT   VARIANT         1195
FT                   /note="N -> S (in dbSNP:rs807547)"
FT                   /id="VAR_059214"
FT   VARIANT         1316
FT                   /note="M -> V (in dbSNP:rs1061325)"
FT                   /id="VAR_059215"
FT   VARIANT         1394
FT                   /note="I -> T (in dbSNP:rs1633399)"
FT                   /id="VAR_059216"
FT   VARIANT         1592
FT                   /note="V -> M (in dbSNP:rs2073738)"
FT                   /id="VAR_059217"
FT   VARIANT         1620
FT                   /note="R -> H (in dbSNP:rs5748024)"
FT                   /id="VAR_059218"
FT   CONFLICT        193
FT                   /note="P -> H (in Ref. 1; AAC50494)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="L -> H (in Ref. 1; AAC50494)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="K -> T (in Ref. 2; CAA64752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        530
FT                   /note="L -> Q (in Ref. 1; AAC50494)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1474
FT                   /note="E -> K (in Ref. 3; AAB40908/AAB40909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1620..1640
FT                   /note="RKQEEHVTEPAPLVFDFDGHE -> PPSKRSM (in Ref. 3;
FT                   AAB40908/AAB40909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1640 AA;  187030 MW;  C661E1AB989D8E7F CRC64;
     MAQILPVRFQ EHFQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV TIIDMSDPMA
     PIRRPISAES AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMAEEVIF WKWVSVNTVA
     LVTETAVYHW SMEGDSQPMK MFDRHTSLVG CQVIHYRTDE YQKWLLLVGI SAQQNRVVGA
     MQLYSVDRKV SQPIEGHAAA FAEFKMEGNA KPATLFCFAV RNPTGGKLHI IEVGQPAAGN
     QPFVKKAVDV FFPPEAQNDF PVAMQIGAKH GVIYLITKYG YLHLYDLESG VCICMNRISA
     DTIFVTAPHK PTSGIIGVNK KGQVLSVCVE EDNIVNYATN VLQNPDLGLR LAVRSNLAGA
     EKLFVRKFNT LFAQGSYAEA AKVAASAPKG ILRTRETVQK FQSIPAQSGQ ASPLLQYFGI
     LLDQGQLNKL ESLELCHLVL QQGRKQLLEK WLKEDKLECS EELGDLVKTT DPMLALSVYL
     RANVPSKVIQ CFAETGQFQK IVLYAKKVGY TPDWIFLLRG VMKISPEQGL QFSRMLVQDE
     EPLANISQIV DIFMENSLIQ QCTSFLLDAL KNNRPAEGLL QTWLLEMNLV HAPQVADAIL
     GNKMFTHYDR AHIAQLCEKA GLLQQALEHY TDLYDIKRAV VHTHLLNPEW LVNFFGSLSV
     EDSVECLHAM LSANIRQNLQ LCVQVASKYH EQLGTQALVE LFESFKSYKG LFYFLGSIVN
     FSQDPDVHLK YIQAACKTGQ IKEVERICRE SSCYNPERVK NFLKEAKLTD QLPLIIVCDR
     FGFVHDLVLY LYRNNLQRYI EIYVQKVNPS RTPAVIGGLL DVDCSEEVIK HLIMAVRGQF
     STDELVAEVE KRNRLKLLLP WLESQIQEGC EEPATHNALA KIYIDSNNSP ECFLRENAYY
     DSSVVGRYCE KRDPHLACVA YERGQCDLEL IKVCNENSLF KSEARYLVCR KDPELWAHVL
     EETNPSRRQL IDQVVQTALS ETRDPEEISV TVKAFMTADL PNELIELLEK IVLDNSVFSE
     HRNLQNLLIL TAIKADRTRV MEYISRLDNY DALDIASIAV SSALYEEAFT VFHKFDMNAS
     AIQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAQAQLQKDL VKEAINSYIR GDDPSSYLEV
     VQSASRSNNW EDLVKFLQMA RKKGRESYIE TELIFALAKT SRVSELEDFI NGPNNAHIQQ
     VGDRCYEEGM YEAAKLLYSN VSNFARLAST LVHLGEYQAA VDNSRKASST RTWKEVCFAC
     MDGQEFRFAQ LCGLHIVIHA DELEELMCYY QDRGYFEELI LLLEAALGLE RAHMGMFTEL
     AILYSKFKPQ KMLEHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAVLTMMS
     HPTEAWKEGQ FKDIITKVAN VELCYRALQF YLDYKPLLIN DLLLVLSPRL DHTWTVSFFS
     KAGQLPLVKP YLRSVQSHNN KSVNEALNHL LTEEEDYQGL RASIDAYDNF DNISLAQQLE
     KHQLMEFRCI AAYLYKGNNW WAQSVELCKK DHLYKDAMQH AAESRDAELA QKLLQWFLEE
     GKRECFAACL FTCYDLLRPD MVLELAWRHN LVDLAMPYFI QVMREYLSKV DKLDALESLR
     KQEEHVTEPA PLVFDFDGHE
//