ID   COCA1_MOUSE             Reviewed;        3120 AA.
AC   Q60847; P70322;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 3.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Collagen alpha-1(XII) chain;
DE   Flags: Precursor;
GN   Name=Col12a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING (ISOFORMS
RP   1 AND 3).
RC   STRAIN=C57BL/6J, and Swiss Webster; TISSUE=Skin;
RX   PubMed=8601036; DOI=10.1002/aja.1002040409;
RA   Boehme K., Li Y., Oh P.S., Olsen B.R.;
RT   "Primary structure of the long and short splice variants of mouse collagen
RT   XII and their tissue-specific expression during embryonic development.";
RL   Dev. Dyn. 204:432-445(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3047-3120, AND ALTERNATIVE SPLICING (ISOFORMS
RP   2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Skin fibroblast;
RX   PubMed=10419532; DOI=10.1074/jbc.274.31.22053;
RA   Kania A.M., Reichenberger E., Baur S.T., Karimbux N.Y., Taylor R.W.,
RA   Olsen B.R., Nishimura I.;
RT   "Structural variation of type XII collagen at its carboxyl-terminal NC1
RT   domain generated by tissue-specific alternative splicing.";
RL   J. Biol. Chem. 274:22053-22059(1999).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21670218; DOI=10.1083/jcb.201010010;
RA   Izu Y., Sun M., Zwolanek D., Veit G., Williams V., Cha B., Jepsen K.J.,
RA   Koch M., Birk D.E.;
RT   "Type XII collagen regulates osteoblast polarity and communication during
RT   bone formation.";
RL   J. Cell Biol. 193:1115-1130(2011).
CC   -!- FUNCTION: Type XII collagen interacts with type I collagen-containing
CC       fibrils, the COL1 domain could be associated with the surface of the
CC       fibrils, and the COL2 and NC3 domains may be localized in the
CC       perifibrillar matrix. {ECO:0000250}.
CC   -!- SUBUNIT: Trimer of identical chains each containing 190 kDa of non-
CC       triple-helical sequences. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=The final tissue form of collagen XII may contain homotrimers
CC         or any combination of the various isoforms.;
CC       Name=1; Synonyms=XIIA-1;
CC         IsoId=Q60847-1; Sequence=Displayed;
CC       Name=2; Synonyms=ER#K, XIIA-2;
CC         IsoId=Q60847-2; Sequence=VSP_001151, VSP_001152;
CC       Name=3; Synonyms=XIIB-1;
CC         IsoId=Q60847-3; Sequence=VSP_001150;
CC       Name=4; Synonyms=XIIB-2;
CC         IsoId=Q60847-4; Sequence=VSP_001150, VSP_001151, VSP_001152;
CC       Name=5;
CC         IsoId=Q60847-5; Sequence=VSP_023404, VSP_023405;
CC   -!- TISSUE SPECIFICITY: Highest expression in tendons, perichondrium, skin,
CC       cornea, sclera, blood vessels, and periosteum.
CC   -!- DEVELOPMENTAL STAGE: The long NC3 XIIA isoforms are predominant at
CC       early stages (ED7 and 11); at later stages of development (ED15 and 17)
CC       the short NC3 XIIB forms become the major forms. As the short NC3 forms
CC       become the major product, the long splice variant continues to be
CC       expressed in several tissues, even after birth. The long NC1 isoforms,
CC       XIIA-1 and XIIB-1, peak in 15-day old embryos and decrease in 17-day
CC       old ones. The expression of the short NC1 form XIIB-2 remains constant
CC       throughout late stages of embryonic development (ED15 and ED17).
CC   -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC       end. {ECO:0000250}.
CC   -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC       is most likely to be 4-hydroxy as this fits the requirement for 4-
CC       hydroxylation in vertebrates. {ECO:0000250}.
CC   -!- PTM: O-glycosylation of isoform 2; glycosaminoglycan of chondroitin-
CC       sulfate type. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Animals have fragile bones with a disorganized
CC       collagen fiber arrangement, decreased expression of bone matrix
CC       proteins, and decreased bone-forming activity associated with delayed
CC       terminal differentiation. They have also decreased grip strength, a
CC       delay in fiber-type transition, and a deficiency in passive force
CC       generation, while the muscle seemed more resistant to eccentric
CC       contraction-induced force drop, indicating a role for a matrix-based
CC       passive force-transducing elastic element in the generation of the
CC       weakness. {ECO:0000269|PubMed:21670218}.
CC   -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC       helices (FACIT) family. {ECO:0000305}.
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DR   EMBL; U25652; AAA99719.1; -; mRNA.
DR   EMBL; AC157477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U57095; AAB07047.1; -; mRNA.
DR   CCDS; CCDS72284.1; -. [Q60847-2]
DR   PIR; C44479; C44479.
DR   PIR; D44479; D44479.
DR   RefSeq; NP_001277237.1; NM_001290308.1. [Q60847-2]
DR   SMR; Q60847; -.
DR   BioGRID; 198807; 3.
DR   ComplexPortal; CPX-2978; Collagen type XII trimer.
DR   STRING; 10090.ENSMUSP00000071662; -.
DR   GlyCosmos; Q60847; 8 sites, No reported glycans.
DR   GlyGen; Q60847; 9 sites.
DR   iPTMnet; Q60847; -.
DR   PhosphoSitePlus; Q60847; -.
DR   SwissPalm; Q60847; -.
DR   CPTAC; non-CPTAC-3417; -.
DR   EPD; Q60847; -.
DR   jPOST; Q60847; -.
DR   MaxQB; Q60847; -.
DR   PaxDb; 10090-ENSMUSP00000071662; -.
DR   PeptideAtlas; Q60847; -.
DR   ProteomicsDB; 283780; -. [Q60847-1]
DR   ProteomicsDB; 283781; -. [Q60847-2]
DR   ProteomicsDB; 283782; -. [Q60847-3]
DR   ProteomicsDB; 283783; -. [Q60847-4]
DR   ProteomicsDB; 283784; -. [Q60847-5]
DR   Pumba; Q60847; -.
DR   Antibodypedia; 2124; 113 antibodies from 20 providers.
DR   DNASU; 12816; -.
DR   Ensembl; ENSMUST00000071750.13; ENSMUSP00000071662.7; ENSMUSG00000032332.18. [Q60847-2]
DR   GeneID; 12816; -.
DR   KEGG; mmu:12816; -.
DR   UCSC; uc009qus.2; mouse. [Q60847-2]
DR   AGR; MGI:88448; -.
DR   CTD; 1303; -.
DR   MGI; MGI:88448; Col12a1.
DR   VEuPathDB; HostDB:ENSMUSG00000032332; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000154923; -.
DR   HOGENOM; CLU_000467_0_0_1; -.
DR   InParanoid; Q60847; -.
DR   OMA; WKRPPDE; -.
DR   OrthoDB; 5353225at2759; -.
DR   PhylomeDB; Q60847; -.
DR   TreeFam; TF329914; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   BioGRID-ORCS; 12816; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Col12a1; mouse.
DR   PRO; PR:Q60847; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q60847; Protein.
DR   Bgee; ENSMUSG00000032332; Expressed in diaphysis of femur and 183 other cell types or tissues.
DR   ExpressionAtlas; Q60847; baseline and differential.
DR   GO; GO:0005595; C:collagen type XII trimer; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0035987; P:endodermal cell differentiation; IBA:GO_Central.
DR   CDD; cd00063; FN3; 18.
DR   CDD; cd01482; vWA_collagen_alphaI-XII-like; 4.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 18.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 4.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF20; COLLAGEN ALPHA-1(XXI) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF00041; fn3; 18.
DR   Pfam; PF00092; VWA; 4.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00060; FN3; 18.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00327; VWA; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 10.
DR   SUPFAM; SSF53300; vWA-like; 4.
DR   PROSITE; PS50853; FN3; 18.
DR   PROSITE; PS50234; VWFA; 4.
DR   Genevisible; Q60847; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Collagen; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..3120
FT                   /note="Collagen alpha-1(XII) chain"
FT                   /id="PRO_0000005784"
FT   DOMAIN          27..117
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          140..316
FT                   /note="VWFA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          336..426
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          440..616
FT                   /note="VWFA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          634..723
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          725..816
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          817..905
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          907..998
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1000..1087
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1089..1179
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1199..1371
FT                   /note="VWFA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          1387..1475
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1476..1567
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1568..1658
FT                   /note="Fibronectin type-III 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1659..1754
FT                   /note="Fibronectin type-III 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1757..1851
FT                   /note="Fibronectin type-III 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1852..1937
FT                   /note="Fibronectin type-III 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1938..2028
FT                   /note="Fibronectin type-III 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2029..2119
FT                   /note="Fibronectin type-III 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2120..2208
FT                   /note="Fibronectin type-III 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2209..2296
FT                   /note="Fibronectin type-III 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2325..2498
FT                   /note="VWFA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          2522..2714
FT                   /note="Laminin G-like"
FT   DOMAIN          2749..2800
FT                   /note="Collagen-like 1"
FT   DOMAIN          2804..2854
FT                   /note="Collagen-like 2"
FT   DOMAIN          2855..2899
FT                   /note="Collagen-like 3"
FT   DOMAIN          2943..2992
FT                   /note="Collagen-like 4"
FT   REGION          1074..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2293..2313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2453..2748
FT                   /note="Nonhelical region (NC3)"
FT   REGION          2749..2900
FT                   /note="Triple-helical region (COL2) with 1 imperfection"
FT   REGION          2752..2898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2901..2943
FT                   /note="Nonhelical region (NC2)"
FT   REGION          2933..3072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2944..3046
FT                   /note="Triple-helical region (COL1) with 2 imperfections"
FT   REGION          3047..3120
FT                   /note="Nonhelical region (NC1)"
FT   REGION          3094..3120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           862..864
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2781..2783
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2897..2899
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1076..1099
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2299..2313
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2780..2799
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2826..2840
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2942..2956
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3020..3038
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3098..3114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2946
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2949
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2952
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2961
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2967
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2970
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2973
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2985
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3002
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3005
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3016
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3025
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3028
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3031
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        329
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99715"
FT   CARBOHYD        700
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        798
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        889
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        981
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1765
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2681
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         25..1186
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001150"
FT   VAR_SEQ         3063..3068
FT                   /note="EPYVPE -> GMLLPS (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8601036"
FT                   /id="VSP_023404"
FT   VAR_SEQ         3063..3065
FT                   /note="EPY -> GSG (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001151"
FT   VAR_SEQ         3066..3120
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001152"
FT   VAR_SEQ         3069..3120
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8601036"
FT                   /id="VSP_023405"
FT   CONFLICT        245
FT                   /note="A -> G (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="K -> KTQPK (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="I -> T (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        552
FT                   /note="K -> E (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611
FT                   /note="E -> V (in Ref. 1; AAB07047/AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        690
FT                   /note="N -> S (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        797
FT                   /note="S -> P (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        954
FT                   /note="P -> N (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1079
FT                   /note="G -> R (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1271
FT                   /note="Y -> N (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1472
FT                   /note="T -> A (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1524
FT                   /note="G -> E (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1773
FT                   /note="V -> I (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1831
FT                   /note="D -> G (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1939
FT                   /note="A -> S (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2005
FT                   /note="N -> Y (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2428..2429
FT                   /note="PK -> R (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2432
FT                   /note="V -> G (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2515
FT                   /note="L -> Q (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2551..2552
FT                   /note="SY -> DS (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2861..2864
FT                   /note="Missing (in Ref. 1; AAA99719)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3120 AA;  340214 MW;  C4D9264E3C5C8CB5 CRC64;
     MQTRLPRALA ALGVALLLSS IEAEVDPPSD LNFKIIDENT VHMSWERPVD PIVGYRITVD
     PTTDGPTKEF TLAASTTETL LSDLIPETQY VVTITSYNEV EESVPVIGQL TIQTGGPTKP
     GEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIVALVSAF DIGEEKTRVG
     VVQYSSDTRT EFNLNQYYRR EDLLAAVKKI PYKGGNTMTG DAIDYLVKNT FTESAGSRAG
     FPKVAIIITD GKSQDEVEIP ARELRNIGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA
     NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVIEPPSNL VVTELSSKYI RLSWDPSPSA
     VTGYKILLTP MAAGSRHHAL SVGPQTTTLN VRDLTADTEY QISVFAMKGL TSSEPTSVME
     KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLAKSF EISPNRVQIS
     LVQYSRDPHT EFTLKEFNRV EDIIKAINTF PYRGGSTNTG KAMTYVREKI FVPNKGSRSN
     VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE
     DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLRF TQVTANSFKA EWSPPGDNVF
     SYHVTYKDAN GDDEVTVVEP ASSTSVVLNN LRPETLYLVN VTAEYEDGFS VPITGEETTA
     EVKGVPRNLK VTDETTDSFK LTWSQAPGRV LRYRIRYRPV SGGESKEVST PANQRRKTLE
     NLTPDTKYEI SVIAEYSSGP GSPLTGNAAT EEVRGNPRDL RVSDATTSTL KLSWSRAPGK
     VKQYLVTYTP AAGGETQEVT VRGDTTTTML RKLKEGTQYD LSVTALYASG AGEALSGKGS
     TLEERGSPQN LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDIEAGE TTLPGDAIHT
     MIENLQPETK YKISVFATYS SGEGEPVTGD ATTELSQDSK ILRVDEETEH TMRVTWKAAP
     GKVVNYRVVY RPQGGGRQMV AKVPPTVTST VLKRLQPQTT YDITVLPMYK TGEGKLRQGS
     GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVLGPYDN
     TVVLEELRAG TTYRVNVFGM FDGGESLPLV GQEMTTLSDT TVTPFLSSGM DCLTRAEADI
     VLLVDGSWSI GRANFRTVRS FISRIVEVFE IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK
     SLLQAVANLP YKGGNTLTGM ALNFIRQQSF KTQAGMRPRA RKIGVLITDG KSQDDVEAPS
     KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSKIVDD LTINLCNSVK
     GPGDLEAPTN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRLDTSTV
     LKDLKPETDY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA
     TGYTVSYQPT RSPEGTKPKE MRVGPTVNDV QLTGLLPNTE YEVTVQAVLY DLTSEPAKAR
     EVTLPLPRPQ DVKLRDVTHS TMNVVWEPVL GKVRKYIVRY KTPDEEFKEV EVDRSRASTI
     LKDLSSQTQY TVSVSAVYDE GTSPPATAYD TTRRVPAPTN LQFTEVTPES FRGTWDHGAS
     DVSLYRITWA PVGNPDKMET ILNGDENTLV FENLNPNTPY EVSITAIYPD ESESEDLSGT
     ERTLRLIPLT TQAPKSGPRN LQVYNATSNS LTVKWDPASG RVQKYRITYQ PSTGEGNEQT
     ITVGGRQNSV LLQKLKPDTP YTITVYSQYP DGEGGRMTGR GKTKPLNTVR NLRVYDPSTS
     SLSVRWDHAE GNPRQYKLFY APTSGGPEEL VPIPGNTNYA ILRNLQPDTP YTITVVPVYT
     EGDGGRTSDT GRTLVRGLAR NIQVYNPTPN SLDVRWDPAP GPVQQYRIVY SPVAGTRPSE
     SIVVPGNTRT VHLERLIPDT PYSVNIVALY SDGEGNPSPS QGRTLPRSGP RNIRVFGETT
     NSLSVAWDHA DGPVQQYRII YSPTVGDPID EYTTVPGRRN NVILQPLQPD TPYKITVIAI
     YEDGDGGHLT GNGRTVGLLP PQNIHIFDEW YTRFRVSWDP SPSPVLGYKI VYKPVGSNEP
     MEAFVGEVTS YTLHNLNPST TYDVSVYAQY DSGLSVPLTD QGTTLYLNVT DLKTYQVGWD
     TFCVKWSPHR AATSYRLKLS PADGTRGQEI TVRGSETSHC FTGLSPEAEY GVTVFVQTPN
     LEGPGVPIKE QTTVKPTEAP TEPPTPSPPP TIPPARDVCK GAKADIVFLT DASWSIGDDN
     FNKVVKFIFN TVGAFDEVNP AGIQVSFVQY SDEVKSEFKL NTYNDKALAL GALQNIRYRG
     GNTRTGKALT FIKEKVLTWE SGMRKNVPKV LVVVTDGRSQ DEVKKAAFVI QQSGFSVFVV
     GVADVDYNEL ANIASKPSER HVFIVDDFES FEKIEDNLIT FVCETATSSC PLIYLDGYTS
     PGFKMLEAYN LTEKNFASVQ GVSLESGSFP SYSAYRLQKN AFINQPTAEL HPNGLPPSYT
     IILLFRLLPE TPSDPFAIWQ ITDRDYRPQV GVIADPSSKT LSFFNKDTRG EVQTVTFDTD
     EVKTLFYGSF HKVHIVVTSK SVKIYIDCYE IIEKDIKEAG NITTDGYEIL GKLLKGERKS
     ATFQIQSFDI VCSPVWTSRD RCCDIPSRRD EAKCPALPNA CTCTQDSVGP PGPPGPAGGP
     GAKGPRGERG INGAVGPPGP RGDTGPPGPQ GPPGPQGPNG LSIPGEQGRQ GMKGDAGEPG
     LPGRTGTPGL PGPPGPMGPP GDRGFTGKDG AMGPRGPPGP PGSPGSPGVT GPSGKPGKPG
     DHGRPGQSGL KGEKGDRGDI ASQNMMRAVA RQVCEQLISG QMSRFNQMLN QIPNDYHSSR
     NQPGPPGPPG PPGSAGARGE PGPGGRPGFP GTPGMQGPPG ERGLPGEKGE RGTGSQGPRG
     PPGPPGPQGE SRTGPPGSTG SRGPPGPPGR PGNSGIRGPP GPPGYCDSSQ CASIPYNGQG
     YPEPYVPEGG AYLPEREPFI VPVEPERTAE YEDDYGADEP DQQHPDHMRW RRALRPGPAE
//