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Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]

 CO2A1_MOUSE             Reviewed;        1487 AA.
P28481; Q61428; Q62031; Q62032; Q62033; Q641K3; Q6LDB1; Q6LDI8;
Q6LDI9; Q80VY3; Q80X38; Q8CEF7; Q8K0N6;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
07-JUN-2017, entry version 170.
RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
AltName: Full=Alpha-1 type II collagen {ECO:0000250|UniProtKB:P02458};
Contains:
RecName: Full=Collagen alpha-1(II) chain {ECO:0000250|UniProtKB:P02458};
Contains:
RecName: Full=Chondrocalcin {ECO:0000250|UniProtKB:P02458};
Flags: Precursor;
Name=Col2a1 {ECO:0000312|MGI:MGI:88452};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=1885613;
Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
"Mouse type II collagen gene. Complete nucleotide sequence, exon
structure, and alternative splicing.";
J. Biol. Chem. 266:16862-16869(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND DEVELOPMENTAL STAGE.
PubMed=1879363;
Cheah K.S., Lau E.T., Au P.K., Tam P.P.;
"Expression of the mouse alpha 1(II) collagen gene is not restricted
to cartilage during development.";
Development 111:945-953(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28; 1031-1145 AND 1359-1487.
PubMed=1797232; DOI=10.1007/BF00351064;
Cheah K.S., Au P.K., Lau E.T., Little P.F., Stubbs L.;
"The mouse Col2a-1 gene is highly conserved and is linked to Int-1 on
chromosome 15.";
Mamm. Genome 1:171-183(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 597-1487.
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1483-1487.
PubMed=2054384;
Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
"Specific hybridization probes for mouse type I, II, III and IX
collagen mRNAs.";
Biochim. Biophys. Acta 1089:241-243(1991).
[7]
VARIANT SEDC CYS-989.
PubMed=12968670; DOI=10.1359/jbmr.2003.18.9.1612;
Donahue L.R., Chang B., Mohan S., Miyakoshi N., Wergedal J.E.,
Baylink D.J., Hawes N.L., Rosen C.J., Ward-Bailey P., Zheng Q.Y.,
Bronson R.T., Johnson K.R., Davisson M.T.;
"A missense mutation in the mouse Col2a1 gene causes
spondyloepiphyseal dysplasia congenita, hearing loss, and
retinoschisis.";
J. Bone Miner. Res. 18:1612-1621(2003).
-!- FUNCTION: Type II collagen is specific for cartilaginous tissues.
It is essential for the normal embryonic development of the
skeleton, for linear growth and for the ability of cartilage to
resist compressive forces.
-!- SUBUNIT: Homotrimers of alpha 1(II) chains.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-738477, EBI-738477;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=P28481-3; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2; Synonyms=Long;
IsoId=P28481-1; Sequence=VSP_022782;
Name=3; Synonyms=Short;
IsoId=P28481-2; Sequence=VSP_022780, VSP_022782;
Name=4;
IsoId=P28481-4; Sequence=VSP_022781, VSP_022784;
Name=5;
IsoId=P28481-5; Sequence=VSP_022783, VSP_022785;
Name=6;
IsoId=P28481-6; Sequence=VSP_022781, VSP_022785;
Name=7;
IsoId=P28481-7; Sequence=VSP_022780;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Expressed in chondrogenic tissues in advance
of chondrocyte differentiation. Expressed early in embryogenesis
at 9.5 days both in the cranial mesenchyme destined for the
chondrocranium, and the sclerotome of the somites, and at 12.5
days in the primordia of the hyoid and the laryngeal cartilage.
Detected in all the chondrogenic tissues of the axial and
appendicular skeleton until the onset of endochondral
ossification. Expression also observed in non-chondrogenic tissues
such as the notochord. Also expressed much later in the tail
tendon, at 16.5-18.5 days. Transiently expressed in the heart at
9.5-12.5 days, the epidermis at 10.5-14.5 days, the calvarial
mesenchyme at 12.5-16.5 days, the inner ear at 14.5 days and the
fetal brain from 9.5-14.5 days. Within the neural tube, expression
is localized to the proliferative ventricular cells of the
forebrain and midbrain of 9.5-10.5 day embryos, and subsequently,
restricted to the rhombencephalic basal plate, the ventricular
layer of the hindbrain and the cervical spinal cord.
{ECO:0000269|PubMed:1879363}.
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: Probably 3-hydroxylated on prolines by LEPREL1 (By
similarity). Proline residues at the third position of the
tripeptide repeating unit (G-X-P) are hydroxylated in some or all
of the chains. Proline residues at the second position of the
tripeptide repeating unit (G-P-X) are hydroxylated in some of the
chains. {ECO:0000250}.
-!- DISEASE: Note=Defects in Col2a1 are the cause of a phenotype
resembling human spondyloepiphyseal dysplasia congenita (sedc).
Homozygous sedc mice can be identified at birth by their small
size and shortened trunk. Adults have shortened noses, dysplastic
vertebrae, femora and tibias, and retinoschisis and hearing loss.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- SEQUENCE CAUTION:
Sequence=BAC25865.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M65161; AAA68099.1; -; Genomic_DNA.
EMBL; M65161; AAA68100.1; -; Genomic_DNA.
EMBL; M65161; AAA68101.1; -; Genomic_DNA.
EMBL; M65161; AAA68102.1; -; Genomic_DNA.
EMBL; BC030913; AAH30913.1; -; mRNA.
EMBL; BC051383; AAH51383.1; -; mRNA.
EMBL; BC052326; AAH52326.1; -; mRNA.
EMBL; BC082331; AAH82331.1; -; mRNA.
EMBL; S63190; AAB19627.1; -; Genomic_DNA.
EMBL; M63708; AAA37436.1; -; Genomic_DNA.
EMBL; M63709; AAC06113.1; -; Genomic_DNA.
EMBL; M63710; AAA37435.1; -; Genomic_DNA.
EMBL; AK028295; BAC25865.1; ALT_INIT; mRNA.
EMBL; X57982; CAA41047.1; -; Genomic_DNA.
CCDS; CCDS37189.2; -. [P28481-3]
CCDS; CCDS49716.1; -. [P28481-7]
PIR; A41182; A41182.
PIR; B41182; B41182.
RefSeq; NP_001106987.2; NM_001113515.2. [P28481-7]
RefSeq; NP_112440.2; NM_031163.3. [P28481-3]
UniGene; Mm.2423; -.
PDB; 2W65; X-ray; 2.21 A; E=530-538.
PDB; 4BKL; X-ray; 3.25 A; E/F/G=744-780.
PDBsum; 2W65; -.
PDBsum; 4BKL; -.
ProteinModelPortal; P28481; -.
SMR; P28481; -.
IntAct; P28481; 1.
STRING; 10090.ENSMUSP00000023123; -.
iPTMnet; P28481; -.
PhosphoSitePlus; P28481; -.
PaxDb; P28481; -.
PeptideAtlas; P28481; -.
PRIDE; P28481; -.
Ensembl; ENSMUST00000023123; ENSMUSP00000023123; ENSMUSG00000022483. [P28481-3]
Ensembl; ENSMUST00000088355; ENSMUSP00000085693; ENSMUSG00000022483. [P28481-7]
GeneID; 12824; -.
KEGG; mmu:12824; -.
UCSC; uc007xlp.2; mouse. [P28481-3]
UCSC; uc007xlq.2; mouse. [P28481-7]
CTD; 1280; -.
MGI; MGI:88452; Col2a1.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410ZVV2; LUCA.
GeneTree; ENSGT00840000129673; -.
HOVERGEN; HBG004933; -.
InParanoid; P28481; -.
KO; K19719; -.
OMA; PLQYMRA; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P28481; -.
TreeFam; TF344135; -.
Reactome; R-MMU-1442490; Collagen degradation.
Reactome; R-MMU-1474244; Extracellular matrix organization.
Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-MMU-186797; Signaling by PDGF.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-MMU-216083; Integrin cell surface interactions.
Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-MMU-3000178; ECM proteoglycans.
Reactome; R-MMU-419037; NCAM1 interactions.
Reactome; R-MMU-8874081; MET activates PTK2 signaling.
Reactome; R-MMU-8948216; Collagen chain trimerization.
ChiTaRS; Col2a1; mouse.
EvolutionaryTrace; P28481; -.
PRO; PR:P28481; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022483; -.
CleanEx; MM_COL2A1; -.
ExpressionAtlas; P28481; baseline and differential.
Genevisible; P28481; MM.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0005581; C:collagen trimer; IDA:MGI.
GO; GO:0005585; C:collagen type II trimer; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042289; F:MHC class II protein binding; ISO:MGI.
GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0001502; P:cartilage condensation; IMP:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
GO; GO:0071773; P:cellular response to BMP stimulus; IDA:MGI.
GO; GO:0007417; P:central nervous system development; IEP:UniProtKB.
GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
GO; GO:0060272; P:embryonic skeletal joint morphogenesis; ISO:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
GO; GO:0060174; P:limb bud formation; IEP:UniProtKB.
GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0030903; P:notochord development; IEP:UniProtKB.
GO; GO:0001503; P:ossification; IEP:UniProtKB.
GO; GO:0071599; P:otic vesicle development; IEP:UniProtKB.
GO; GO:0060021; P:palate development; IMP:MGI.
GO; GO:0006029; P:proteoglycan metabolic process; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
GO; GO:0001501; P:skeletal system development; ISO:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
GO; GO:0007601; P:visual perception; ISO:MGI.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 10.
Pfam; PF00093; VWC; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00214; VWC; 1.
PROSITE; PS51461; NC1_FIB; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Collagen;
Complete proteome; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 181 N-terminal propeptide. {ECO:0000250}.
/FTId=PRO_0000005732.
CHAIN 182 1241 Collagen alpha-1(II) chain.
/FTId=PRO_0000005733.
CHAIN 1242 1487 Chondrocalcin.
/FTId=PRO_0000005734.
DOMAIN 32 89 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1253 1487 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 201 1214 Triple-helical region.
REGION 1215 1241 Nonhelical region (C-terminal).
METAL 1301 1301 Calcium. {ECO:0000250}.
METAL 1303 1303 Calcium. {ECO:0000250}.
METAL 1304 1304 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1306 1306 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1309 1309 Calcium. {ECO:0000250}.
SITE 181 182 Cleavage; by procollagen N-endopeptidase.
{ECO:0000250}.
SITE 1241 1242 Cleavage; by procollagen C-endopeptidase.
{ECO:0000250}.
MOD_RES 190 190 5-hydroxylysine. {ECO:0000250}.
MOD_RES 287 287 5-hydroxylysine. {ECO:0000250}.
MOD_RES 299 299 5-hydroxylysine. {ECO:0000250}.
MOD_RES 308 308 5-hydroxylysine. {ECO:0000250}.
MOD_RES 374 374 5-hydroxylysine. {ECO:0000250}.
MOD_RES 608 608 5-hydroxylysine. {ECO:0000250}.
MOD_RES 620 620 5-hydroxylysine. {ECO:0000250}.
MOD_RES 670 670 3-hydroxyproline. {ECO:0000250}.
MOD_RES 907 907 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1144 1144 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1186 1186 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1201 1201 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1207 1207 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1213 1213 3-hydroxyproline. {ECO:0000250}.
CARBOHYD 190 190 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 287 287 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 299 299 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 308 308 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 374 374 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 608 608 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
CARBOHYD 620 620 O-linked (Gal...) hydroxylysine.
{ECO:0000250}.
DISULFID 1283 1315 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1289 1289 Interchain (with C-1306).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1306 1306 Interchain (with C-1289).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1323 1485 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1393 1438 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VAR_SEQ 29 97 QEAGSCLQNGQRYKDKDVWKPSSCRICVCDTGNVLCDDIIC
EDPDCLNPEIPFGECCPICPADLATASG -> R (in
isoform 3 and isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022780.
VAR_SEQ 103 113 Missing (in isoform 4 and isoform 6).
{ECO:0000305}.
/FTId=VSP_022781.
VAR_SEQ 114 142 Missing (in isoform 2 and isoform 3).
{ECO:0000305}.
/FTId=VSP_022782.
VAR_SEQ 114 124 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_022783.
VAR_SEQ 125 142 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_022784.
VAR_SEQ 143 177 Missing (in isoform 5 and isoform 6).
{ECO:0000305}.
/FTId=VSP_022785.
VARIANT 989 989 R -> C (in sedc mice).
{ECO:0000269|PubMed:12968670}.
CONFLICT 97 97 G -> GR (in Ref. 1; AAA68100/AAA68101/
AAA68099/AAA68102). {ECO:0000305}.
CONFLICT 272 272 Q -> M (in Ref. 1; AAA68100/AAA68101/
AAA68099/AAA68102). {ECO:0000305}.
CONFLICT 539 539 T -> A (in Ref. 1; AAA68100/AAA68101/
AAA68099/AAA68102). {ECO:0000305}.
CONFLICT 806 806 V -> A (in Ref. 1; AAA68100/AAA68101/
AAA68099/AAA68102). {ECO:0000305}.
CONFLICT 824 824 R -> P (in Ref. 1; AAA68100/AAA68101/
AAA68099). {ECO:0000305}.
CONFLICT 947 947 Q -> E (in Ref. 1; AAA68100/AAA68101/
AAA68099/AAA68102). {ECO:0000305}.
CONFLICT 1119 1119 G -> R (in Ref. 2; AAH51383).
{ECO:0000305}.
CONFLICT 1141 1145 LPGPP -> SAWPS (in Ref. 4; AAC06113).
{ECO:0000305}.
SEQUENCE 1487 AA; 141973 MW; E52A7F3951C76701 CRC64;
MIRLGAPQSL VLLTLLIAAV LRCQGQDAQE AGSCLQNGQR YKDKDVWKPS SCRICVCDTG
NVLCDDIICE DPDCLNPEIP FGECCPICPA DLATASGKLG PKGQKGEPGD IRDIIGPRGP
PGPQGPAGEQ GPRGDRGDKG EKGAPGPRGR DGEPGTPGNP GPAGPPGPPG PPGLSAGNFA
AQMAGGYDEK AGGAQMGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG
PRGPPGPAGK PGDDGEAGKP GKSGERGLPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG SRGEPGNPGS PGPAGASGNP GTDGIPGAKG
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQAGEPGI AGFKGDQGPK GETGPAGPQG
APGPAGEEGK RGARGEPGGA GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLTG
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
VMGFPGPKGA NGEPGKAGEK GLAGAPGLRG LPGKDGETGA AGPPGPSGPA GERGEQGAPG
PSGFQGLPGP PGPPGEGGKQ GDQGIPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG
LPGTPGTDGP KGAAGPDGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PSGSTGARGA PGERGETGPP GPAGFAGPPG
ADGQPGAKGD QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
AAGRVGPPGA NGNPGPAGPP GPAGKDGPKG VRGDSGPPGR AGDPGLQGPA GAPGEKGEPG
DDGPSGLDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGALGAPGAP GPPGSPGPAG
PTGKQGDRGE AGAQGPMGPS GPAGARGIAG PQGPRGDKGE SGEQGERGLK GHRGFTGLQG
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGSNGI PGPIGPPGPR GRSGETGPVG
PPGSPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPMQYMR ADEADSTLRQ HDVEVDATLK
SLNNQIESIR SPDGSRKNPA RTCQDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG
ETCVYPNPAT VPRKNWWSSK SKEKKHIWFG ETMNGGFHFS YGDGNLAPNT ANVQMTFLRL
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE MRAEGNSRFT YTALKDGCTK
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGAEQEFGVD IGPVCFL


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