CO8A2_HUMAN
ID CO8A2_HUMAN Reviewed; 703 AA.
AC P25067; Q5JV31; Q8TEJ5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Collagen alpha-2(VIII) chain;
DE AltName: Full=Endothelial collagen;
DE Flags: Precursor;
GN Name=COL8A2;
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 [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-703.
RX PubMed=2019595; DOI=10.1016/s0021-9258(20)89508-8;
RA Muragaki Y., Jacenko O., Apte S., Mattei M.-G., Ninomiya Y., Olsen B.R.;
RT "The alpha 2(VIII) collagen gene. A novel member of the short chain
RT collagen family located on the human chromosome 1.";
RL J. Biol. Chem. 266:7721-7727(1991).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1515454; DOI=10.1016/0925-4439(92)90103-t;
RA Kittelberger R., Neale T.J., Francky K.T., Greenhill N.S., Gibson G.J.;
RT "Cleavage of type VIII collagen by human neutrophil elastase.";
RL Biochim. Biophys. Acta 1139:295-299(1992).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10686422; DOI=10.1016/s0945-053x(99)00053-0;
RA Greenhill N.S., Ruger B.M., Hasan Q., Davis P.F.;
RT "The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct
RT homotrimeric proteins in vivo.";
RL Matrix Biol. 19:19-28(2000).
RN [7]
RP SUBUNIT.
RX PubMed=14990571; DOI=10.1074/jbc.m305805200;
RA Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M.;
RT "Expression and supramolecular assembly of recombinant alpha1(viii) and
RT alpha2(viii) collagen homotrimers.";
RL J. Biol. Chem. 279:21469-21477(2004).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17888087; DOI=10.1111/j.1365-2362.2007.01864.x;
RA Gerth J., Cohen C.D., Hopfer U., Lindenmeyer M.T., Sommer M., Grone H.J.,
RA Wolf G.;
RT "Collagen type VIII expression in human diabetic nephropathy.";
RL Eur. J. Clin. Invest. 37:767-773(2007).
RN [9]
RP VARIANTS FECD1 GLN-304; ARG-357; HIS-434; LYS-455 AND LEU-575, VARIANT
RP PPCD2 LYS-455, AND VARIANTS ARG-3; GLN-155 AND ILE-645.
RX PubMed=11689488; DOI=10.1093/hmg/10.21.2415;
RA Biswas S., Munier F.L., Yardley J., Hart-Holden N., Perveen R., Cousin P.,
RA Sutphin J.E., Noble B., Batterbury M., Kielty C., Hackett A., Bonshek R.,
RA Ridgway A., McLeod D., Sheffield V.C., Stone E.M., Schorderet D.F.,
RA Black G.C.M.;
RT "Missense mutations in COL8A2, the gene encoding the alpha-2 chain of type
RT VIII collagen, cause two forms of corneal endothelial dystrophy.";
RL Hum. Mol. Genet. 10:2415-2423(2001).
RN [10]
RP VARIANTS GLN-155 AND MET-502.
RX PubMed=15175909; DOI=10.1007/s10384-003-0063-6;
RA Kobayashi A., Fujiki K., Murakami A., Kato T., Chen L.-Z., Onoe H.,
RA Nakayasu K., Sakurai M., Takahashi M., Sugiyama K., Kanai A.;
RT "Analysis of COL8A2 gene mutation in Japanese patients with Fuchs'
RT endothelial dystrophy and posterior polymorphous dystrophy.";
RL Jpn. J. Ophthalmol. 48:195-198(2004).
CC -!- FUNCTION: Macromolecular component of the subendothelium. Major
CC component of the Descemet's membrane (basement membrane) of corneal
CC endothelial cells. Also a component of the endothelia of blood vessels.
CC Necessary for migration and proliferation of vascular smooth muscle
CC cells and thus, has a potential role in the maintenance of vessel wall
CC integrity and structure, in particular in atherogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha
CC 2(VIII) type collagens. Four homotrimers can form a tetrahedron
CC stabilized by central interacting C-terminal NC1 trimers.
CC {ECO:0000269|PubMed:14990571}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Expressed primarily in the subendothelium of large
CC blood vessels. Also expressed in arterioles and venules in muscle,
CC heart, kidney, spleen, umbilical cord, liver and lung and is also found
CC in connective tissue layers around hair follicles, around nerve bundles
CC in muscle, in the dura of the optic nerve, in cornea and sclera, and in
CC the perichondrium of cartilaginous tissues. In the kidney, expressed in
CC mesangial cells, glomerular endothelial cells, and tubular epithelial
CC cells. Also expressed in mast cells, and in astrocytes during the
CC repair process. Expressed in Descemet's membrane.
CC {ECO:0000269|PubMed:10686422, ECO:0000269|PubMed:17888087}.
CC -!- INDUCTION: Some up-regulation in diabetic nephropathy.
CC {ECO:0000269|PubMed:17888087}.
CC -!- PTM: Proteolytically cleaved by neutrophil elastase, in vitro.
CC {ECO:0000269|PubMed:1515454}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 1 (FECD1) [MIM:136800]:
CC A corneal disease caused by loss of endothelium of the central cornea.
CC It is characterized by focal wart-like guttata that arise from Descemet
CC membrane and develop in the central cornea, epithelial blisters,
CC reduced vision and pain. Descemet membrane is thickened by abnormal
CC collagenous deposition. {ECO:0000269|PubMed:11689488}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Corneal dystrophy, posterior polymorphous, 2 (PPCD2)
CC [MIM:609140]: A rare mild subtype of posterior corneal dystrophy
CC characterized by alterations of Descemet membrane presenting as
CC vesicles, opacities or band-like lesions on slit-lamp examination and
CC specular microscopy. Affected patient typically are asymptomatic.
CC {ECO:0000269|PubMed:11689488}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84955.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK074129; BAB84955.1; ALT_INIT; mRNA.
DR EMBL; AL138787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07388.1; -; Genomic_DNA.
DR EMBL; M60832; AAA62822.1; -; Genomic_DNA.
DR CCDS; CCDS403.1; -.
DR PIR; A57131; A57131.
DR RefSeq; NP_001281276.1; NM_001294347.1.
DR RefSeq; NP_005193.1; NM_005202.3.
DR AlphaFoldDB; P25067; -.
DR SMR; P25067; -.
DR BioGRID; 107693; 45.
DR ComplexPortal; CPX-1745; Collagen type VIII trimer variant 1.
DR ComplexPortal; CPX-1747; Collagen type VIII trimer variant 3.
DR STRING; 9606.ENSP00000380901; -.
DR iPTMnet; P25067; -.
DR PhosphoSitePlus; P25067; -.
DR BioMuta; COL8A2; -.
DR DMDM; 45644957; -.
DR jPOST; P25067; -.
DR MassIVE; P25067; -.
DR PaxDb; P25067; -.
DR PeptideAtlas; P25067; -.
DR PRIDE; P25067; -.
DR ProteomicsDB; 54250; -.
DR Antibodypedia; 56213; 165 antibodies from 24 providers.
DR DNASU; 1296; -.
DR Ensembl; ENST00000303143.9; ENSP00000305913.4; ENSG00000171812.13.
DR Ensembl; ENST00000397799.2; ENSP00000380901.1; ENSG00000171812.13.
DR GeneID; 1296; -.
DR KEGG; hsa:1296; -.
DR MANE-Select; ENST00000397799.2; ENSP00000380901.1; NM_005202.4; NP_005193.1.
DR UCSC; uc001bzv.4; human.
DR CTD; 1296; -.
DR DisGeNET; 1296; -.
DR GeneCards; COL8A2; -.
DR HGNC; HGNC:2216; COL8A2.
DR HPA; ENSG00000171812; Low tissue specificity.
DR MalaCards; COL8A2; -.
DR MIM; 120252; gene.
DR MIM; 136800; phenotype.
DR MIM; 609140; phenotype.
DR neXtProt; NX_P25067; -.
DR OpenTargets; ENSG00000171812; -.
DR Orphanet; 98974; Fuchs endothelial corneal dystrophy.
DR Orphanet; 98973; Posterior polymorphous corneal dystrophy.
DR PharmGKB; PA26732; -.
DR VEuPathDB; HostDB:ENSG00000171812; -.
DR eggNOG; ENOG502QRST; Eukaryota.
DR GeneTree; ENSGT00940000154317; -.
DR InParanoid; P25067; -.
DR OMA; IPHMKYM; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; P25067; -.
DR TreeFam; TF334029; -.
DR PathwayCommons; P25067; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 1296; 16 hits in 1063 CRISPR screens.
DR ChiTaRS; COL8A2; human.
DR GeneWiki; COL8A2; -.
DR GenomeRNAi; 1296; -.
DR Pharos; P25067; Tbio.
DR PRO; PR:P25067; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P25067; protein.
DR Bgee; ENSG00000171812; Expressed in periodontal ligament and 162 other tissues.
DR ExpressionAtlas; P25067; baseline and differential.
DR Genevisible; P25067; HS.
DR GO; GO:0005604; C:basement membrane; NAS:UniProtKB.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Basement membrane; Cell adhesion; Collagen;
KW Corneal dystrophy; Disease variant; Extracellular matrix; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..703
FT /note="Collagen alpha-2(VIII) chain"
FT /id="PRO_0000005835"
FT DOMAIN 570..703
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 29..76
FT /note="Nonhelical region (NC2)"
FT REGION 70..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..536
FT /note="Triple-helical region"
FT REGION 537..703
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 74..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 3
FT /note="G -> R (in dbSNP:rs115156902)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017893"
FT VARIANT 155
FT /note="R -> Q (in dbSNP:rs75864656)"
FT /evidence="ECO:0000269|PubMed:11689488,
FT ECO:0000269|PubMed:15175909"
FT /id="VAR_017894"
FT VARIANT 304
FT /note="R -> Q (in FECD1; dbSNP:rs369487110)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017895"
FT VARIANT 357
FT /note="G -> R (in FECD1; unknown pathological significance;
FT dbSNP:rs199786966)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017896"
FT VARIANT 434
FT /note="R -> H (in FECD1; dbSNP:rs201235688)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017897"
FT VARIANT 455
FT /note="Q -> K (in FECD1 and PPCD2; dbSNP:rs80358191)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017898"
FT VARIANT 502
FT /note="T -> M (in dbSNP:rs117860804)"
FT /evidence="ECO:0000269|PubMed:15175909"
FT /id="VAR_021387"
FT VARIANT 575
FT /note="P -> L (in FECD1; unknown pathological significance;
FT dbSNP:rs145553904)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017899"
FT VARIANT 645
FT /note="T -> I (in dbSNP:rs200767854)"
FT /evidence="ECO:0000269|PubMed:11689488"
FT /id="VAR_017900"
FT CONFLICT 88
FT /note="R -> W (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="M -> H (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> N (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="E -> D (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..378
FT /note="PK -> LR (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="T -> R (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="P -> L (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..531
FT /note="Missing (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="F -> L (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="M -> I (in Ref. 4; AAA62822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 703 AA; 67244 MW; 84BD7CBDBDECD466 CRC64;
MLGTLTPLSS LLLLLLVLVL GCGPRASSGG GAGGAAGYAP VKYIQPMQKG PVGPPFREGK
GQYLEMPLPL LPMDLKGEPG PPGKPGPRGP PGPPGFPGKP GMGKPGLHGQ PGPAGPPGFS
RMGKAGPPGL PGKVGPPGQP GLRGEPGIRG DQGLRGPPGP PGLPGPSGIT IPGKPGAQGV
PGPPGFQGEP GPQGEPGPPG DRGLKGDNGV GQPGLPGAPG QGGAPGPPGL PGPAGLGKPG
LDGLPGAPGD KGESGPPGVP GPRGEPGAVG PKGPPGVDGV GVPGAAGLPG PQGPSGAKGE
PGTRGPPGLI GPTGYGMPGL PGPKGDRGPA GVPGLLGDRG EPGEDGEPGE QGPQGLGGPP
GLPGSAGLPG RRGPPGPKGE AGPGGPPGVP GIRGDQGPSG LAGKPGVPGE RGLPGAHGPP
GPTGPKGEPG FTGRPGGPGV AGALGQKGDL GLPGQPGLRG PSGIPGLQGP AGPIGPQGLP
GLKGEPGLPG PPGEGRAGEP GTAGPTGPPG VPGSPGITGP PGPPGPPGPP GAPGAFDETG
IAGLHLPNGG VEGAVLGKGG KPQFGLGELS AHATPAFTAV LTSPFPASGM PVKFDRTLYN
GHSGYNPATG IFTCPVGGVY YFAYHVHVKG TNVWVALYKN NVPATYTYDE YKKGYLDQAS
GGAVLQLRPN DQVWVQMPSD QANGLYSTEY IHSSFSGFLL CPT
