CHODL_HUMAN
ID CHODL_HUMAN Reviewed; 273 AA.
AC Q9H9P2; B2R9C0; B4DJB8; Q7Z798; Q7Z799; Q7Z7A0; Q9HCY3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Chondrolectin;
DE AltName: Full=Transmembrane protein MT75;
DE Flags: Precursor;
GN Name=CHODL; Synonyms=C21orf68; ORFNames=PRED12, UNQ872/PRO1890;
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), AND TISSUE SPECIFICITY.
RX PubMed=12079284; DOI=10.1006/geno.2002.6806;
RA Weng L., Smits P., Wauters J., Merregaert J.;
RT "Molecular cloning and characterization of human chondrolectin, a novel
RT type I transmembrane protein homologous to C-type lectins.";
RL Genomics 80:62-70(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE PROMOTER USAGE,
RP AND SUBCELLULAR LOCATION (ISOFORMS 2 AND 3).
RX PubMed=12621022; DOI=10.1074/jbc.m300653200;
RA Weng L., Van Bockstaele D.R., Wauters J., Van Marck E., Plum J.,
RA Berneman Z.N., Merregaert J.;
RT "A novel alternative spliced chondrolectin isoform lacking the
RT transmembrane domain is expressed during T cell maturation.";
RL J. Biol. Chem. 278:19164-19170(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S.,
RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the human
RT chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND MISCELLANEOUS.
RX PubMed=22042635; DOI=10.1074/mcp.m111.013458;
RA Uhlen M., Oksvold P., Algenas C., Hamsten C., Fagerberg L., Klevebring D.,
RA Lundberg E., Odeberg J., Ponten F., Kondo T., Sivertsson A.;
RT "Antibody-based protein profiling of the human chromosome 21.";
RL Mol. Cell. Proteomics 11:M111.013458-M111.013458(2012).
CC -!- FUNCTION: May play a role in the development of the nervous system such
CC as in neurite outgrowth and elongation. May be involved in motor axon
CC growth and guidance. {ECO:0000250|UniProtKB:Q568T5,
CC ECO:0000250|UniProtKB:Q9CXM0}.
CC -!- SUBUNIT: Interacts with RABGGTB. {ECO:0000250|UniProtKB:Q9CXM0}.
CC -!- INTERACTION:
CC Q9H9P2; Q92843: BCL2L2; NbExp=3; IntAct=EBI-17447707, EBI-707714;
CC Q9H9P2; Q12982: BNIP2; NbExp=3; IntAct=EBI-17447707, EBI-752094;
CC Q9H9P2; O14523: C2CD2L; NbExp=3; IntAct=EBI-17447707, EBI-12822627;
CC Q9H9P2; Q07325: CXCL9; NbExp=3; IntAct=EBI-17447707, EBI-3911467;
CC Q9H9P2; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-17447707, EBI-8645574;
CC Q9H9P2; Q15125: EBP; NbExp=3; IntAct=EBI-17447707, EBI-3915253;
CC Q9H9P2; P24593: IGFBP5; NbExp=3; IntAct=EBI-17447707, EBI-720480;
CC Q9H9P2; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-17447707, EBI-10317425;
CC Q9H9P2; O95968: SCGB1D1; NbExp=3; IntAct=EBI-17447707, EBI-12825395;
CC Q9H9P2; Q8IVQ6: ZDHHC21; NbExp=3; IntAct=EBI-17447707, EBI-2849773;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22042635}. Membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12621022}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:12621022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H9P2-1; Sequence=Displayed;
CC Name=2; Synonyms=CHODLF;
CC IsoId=Q9H9P2-2; Sequence=VSP_017275;
CC Name=3; Synonyms=CHODLFdeltaE;
CC IsoId=Q9H9P2-3; Sequence=VSP_017275, VSP_017276;
CC Name=4;
CC IsoId=Q9H9P2-4; Sequence=VSP_043300;
CC -!- TISSUE SPECIFICITY: Found in spleen, testis, prostate and fetal liver.
CC Expression limited to vascular muscle of testis, smooth muscle of
CC prostate stroma, heart muscle, skeletal muscle, crypts of small
CC intestine, and red pulp of spleen. B lymphocytes express isoform 2
CC only; peripheral blood T lymphocytes express isoform 3 only;
CC granulocytes and monocytes express neither isoform 2 nor isoform 3.
CC During development of T lymphocytes, bone marrow progenitor cells
CC express isoform 2 only; thymocytes at different stages of maturation
CC express predominantly isoform 2 and weakly isoform 3, and mature
CC thymocytes express only isoform 2. {ECO:0000269|PubMed:11707072,
CC ECO:0000269|PubMed:12079284, ECO:0000269|PubMed:12621022}.
CC -!- PTM: N-glycosylated.
CC -!- MISCELLANEOUS: A protein of the expected size has been detected by
CC antibody binding and Western blot in at least one of the analyzed
CC tissues or cells. {ECO:0000305|PubMed:22042635}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Chondrolectin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_185";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF257472; AAL05981.1; -; mRNA.
DR EMBL; AF523313; AAP43902.1; -; mRNA.
DR EMBL; AF523314; AAP43903.1; -; mRNA.
DR EMBL; AF523315; AAP43904.1; -; mRNA.
DR EMBL; AY358608; AAQ88971.1; -; mRNA.
DR EMBL; AK022689; BAB14181.1; -; mRNA.
DR EMBL; AK296009; BAG58780.1; -; mRNA.
DR EMBL; AK313725; BAG36467.1; -; mRNA.
DR EMBL; AF130417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163217; CAB90388.1; -; Genomic_DNA.
DR EMBL; AP000404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX10018.1; -; Genomic_DNA.
DR EMBL; BC009418; AAH09418.1; -; mRNA.
DR CCDS; CCDS13570.1; -. [Q9H9P2-1]
DR CCDS; CCDS56208.1; -. [Q9H9P2-4]
DR CCDS; CCDS56209.1; -. [Q9H9P2-2]
DR CCDS; CCDS56210.1; -. [Q9H9P2-3]
DR RefSeq; NP_001191103.1; NM_001204174.1. [Q9H9P2-4]
DR RefSeq; NP_001191104.1; NM_001204175.1. [Q9H9P2-2]
DR RefSeq; NP_001191105.1; NM_001204176.1. [Q9H9P2-2]
DR RefSeq; NP_001191106.1; NM_001204177.1.
DR RefSeq; NP_001191107.1; NM_001204178.1.
DR RefSeq; NP_079220.2; NM_024944.2. [Q9H9P2-1]
DR RefSeq; XP_011527759.1; XM_011529457.2. [Q9H9P2-2]
DR AlphaFoldDB; Q9H9P2; -.
DR SMR; Q9H9P2; -.
DR BioGRID; 126628; 33.
DR IntAct; Q9H9P2; 10.
DR STRING; 9606.ENSP00000299295; -.
DR GlyGen; Q9H9P2; 1 site.
DR iPTMnet; Q9H9P2; -.
DR PhosphoSitePlus; Q9H9P2; -.
DR BioMuta; CHODL; -.
DR DMDM; 18202949; -.
DR MassIVE; Q9H9P2; -.
DR PaxDb; Q9H9P2; -.
DR PeptideAtlas; Q9H9P2; -.
DR PRIDE; Q9H9P2; -.
DR ProteomicsDB; 81335; -. [Q9H9P2-1]
DR ProteomicsDB; 81336; -. [Q9H9P2-2]
DR ProteomicsDB; 81337; -. [Q9H9P2-3]
DR ProteomicsDB; 81338; -. [Q9H9P2-4]
DR Antibodypedia; 2518; 135 antibodies from 24 providers.
DR DNASU; 140578; -.
DR Ensembl; ENST00000299295.7; ENSP00000299295.2; ENSG00000154645.14. [Q9H9P2-1]
DR Ensembl; ENST00000400127.5; ENSP00000382992.1; ENSG00000154645.14. [Q9H9P2-2]
DR Ensembl; ENST00000400128.5; ENSP00000382993.1; ENSG00000154645.14. [Q9H9P2-2]
DR Ensembl; ENST00000543733.5; ENSP00000443566.1; ENSG00000154645.14. [Q9H9P2-4]
DR GeneID; 140578; -.
DR KEGG; hsa:140578; -.
DR MANE-Select; ENST00000299295.7; ENSP00000299295.2; NM_024944.3; NP_079220.2.
DR UCSC; uc002ykr.5; human. [Q9H9P2-1]
DR CTD; 140578; -.
DR DisGeNET; 140578; -.
DR GeneCards; CHODL; -.
DR HGNC; HGNC:17807; CHODL.
DR HPA; ENSG00000154645; Tissue enhanced (lymphoid tissue, testis).
DR MIM; 607247; gene.
DR neXtProt; NX_Q9H9P2; -.
DR OpenTargets; ENSG00000154645; -.
DR PharmGKB; PA26475; -.
DR VEuPathDB; HostDB:ENSG00000154645; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00390000001844; -.
DR HOGENOM; CLU_045492_1_0_1; -.
DR InParanoid; Q9H9P2; -.
DR OMA; VASATCC; -.
DR PhylomeDB; Q9H9P2; -.
DR TreeFam; TF330715; -.
DR PathwayCommons; Q9H9P2; -.
DR SignaLink; Q9H9P2; -.
DR BioGRID-ORCS; 140578; 7 hits in 1059 CRISPR screens.
DR ChiTaRS; CHODL; human.
DR GeneWiki; CHODL; -.
DR GenomeRNAi; 140578; -.
DR Pharos; Q9H9P2; Tbio.
DR PRO; PR:Q9H9P2; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9H9P2; protein.
DR Bgee; ENSG00000154645; Expressed in calcaneal tendon and 118 other tissues.
DR ExpressionAtlas; Q9H9P2; baseline and differential.
DR Genevisible; Q9H9P2; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; NAS:HGNC-UCL.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Cytoplasm;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Membrane;
KW Neurogenesis; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..273
FT /note="Chondrolectin"
FT /id="PRO_0000017415"
FT TOPO_DOM 22..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..179
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 248..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 144..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12621022,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_017275"
FT VAR_SEQ 1..27
FT /note="MSRVVSLLLGAALLCGHGAFCRRVVSG -> MTAGSAHS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043300"
FT VAR_SEQ 212..273
FT /note="GIIPNLIYVVIPTIPLLLLILVAFGTCCFQMLHKSKGRTKTSPNQSTLWISK
FT STRKESGMEV -> VKEEQKLVQTSLHCGFQRVPEKKAAWKYNNSLTWFQNFVILDLYK
FT EWHQNNSLEWLEITKDLQDEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12621022"
FT /id="VSP_017276"
FT CONFLICT 56
FT /note="E -> G (in Ref. 2; AAP43902)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="G -> S (in Ref. 2; AAP43902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30431 MW; F4890AAFB572A311 CRC64;
MSRVVSLLLG AALLCGHGAF CRRVVSGQKV CFADFKHPCY KMAYFHELSS RVSFQEARLA
CESEGGVLLS LENEAEQKLI ESMLQNLTKP GTGISDGDFW IGLWRNGDGQ TSGACPDLYQ
WSDGSNSQYR NWYTDEPSCG SEKCVVMYHQ PTANPGLGGP YLYQWNDDRC NMKHNYICKY
EPEINPTAPV EKPYLTNQPG DTHQNVVVTE AGIIPNLIYV VIPTIPLLLL ILVAFGTCCF
QMLHKSKGRT KTSPNQSTLW ISKSTRKESG MEV
