CLH2_HUMAN
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 03-AUG-2022, entry version 199.
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="http://atlasgeneticsoncology.org/Genes/CLTCL1ID361.html";
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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; 224.
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; P53675; -.
DR PeptideAtlas; P53675; -.
DR PRIDE; P53675; -.
DR ProteomicsDB; 56608; -. [P53675-1]
DR ProteomicsDB; 56609; -. [P53675-2]
DR Antibodypedia; 50558; 108 antibodies from 20 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 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; KCNEPAV; -.
DR OrthoDB; 17940at2759; -.
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 1086 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 131 other tissues.
DR ExpressionAtlas; P53675; baseline and differential.
DR Genevisible; P53675; HS.
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; 1.25.40.10; -; 4.
DR Gene3D; 2.130.10.110; -; 1.
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 Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 4.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
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
