ID CO1A2_SCESX Reviewed; 413 AA. AC C0HLI6; DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2019, sequence version 1. DT 02-JUN-2021, entry version 3. DE RecName: Full=Collagen alpha-2(I) chain {ECO:0000303|PubMed:31171860}; DE AltName: Full=Alpha-2 type I collagen {ECO:0000250|UniProtKB:P08123}; DE Flags: Fragments; OS Scelidotherium sp. (strain SLP-2019) (South American ground sloth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Xenarthra; Pilosa; Folivora; Mylodontidae; Scelidotherium; OC unclassified Scelidotherium. OX NCBI_TaxID=2546665 {ECO:0000303|PubMed:31171860}; RN [1] {ECO:0000305} RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Bone {ECO:0000303|PubMed:31171860}; RX PubMed=31171860; DOI=10.1038/s41559-019-0909-z; RA Presslee S., Slater G.J., Pujos F., Forasiepi A.M., Fischer R., Molloy K., RA Mackie M., Olsen J.V., Kramarz A., Taglioretti M., Scaglia F., Lezcano M., RA Lanata J.L., Southon J., Feranec R., Bloch J., Hajduk A., Martin F.M., RA Salas Gismondi R., Reguero M., de Muizon C., Greenwood A., Chait B.T., RA Penkman K., Collins M., MacPhee R.D.E.; RT "Palaeoproteomics resolves sloth relationships."; RL Nat. Ecol. Evol. 0:0-0(2019). CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar CC forming collagen). {ECO:0000305}. CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space. CC Secreted, extracellular space, extracellular matrix {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in bones. {ECO:0000269|PubMed:31171860}. 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 {ECO:0000250|UniProtKB:P08123}. CC -!- MISCELLANEOUS: These protein fragments were extracted from an ancient CC phalanx bone collected at Arroyo Del Moro in Argentina. CC {ECO:0000269|PubMed:31171860}. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. {ECO:0000305}. 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 GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR InterPro; IPR008160; Collagen. DR Pfam; PF01391; Collagen; 4. PE 1: Evidence at protein level; KW Direct protein sequencing; Extinct organism protein; Extracellular matrix; KW Glycoprotein; Hydroxylation; Secreted. FT CHAIN 1..413 FT /note="Collagen alpha-2(I) chain" FT /id="PRO_0000448461" FT REGION 1..413 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 132..146 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 7 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P08123" FT MOD_RES 10 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P08123" FT MOD_RES 21 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P08123" FT MOD_RES 27 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P08123" FT MOD_RES 82 FT /note="5-hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08123" FT MOD_RES 313 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P08123" FT MOD_RES 316 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250|UniProtKB:P08123" FT CARBOHYD 82 FT /note="O-linked (Gal...) hydroxylysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08123" FT UNSURE 6 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 14 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 78 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 102 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 151 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 170 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 188 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 197 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 206 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 216 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 270 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 279 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 318 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 324 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 342 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 386 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT UNSURE 407 FT /note="L or I" FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 12..13 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 53..54 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 61..62 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 82..83 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 159..160 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 210..211 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_CONS 378..379 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_TER 1 FT /evidence="ECO:0000303|PubMed:31171860" FT NON_TER 413 FT /evidence="ECO:0000303|PubMed:31171860" SQ SEQUENCE 413 AA; 37111 MW; BD8184C4CA899B13 CRC64; FDFSFLPQPP QEGLMGPRGP PGASGAPGPQ GFQGPAGEPG EPGQTGPAGA RGPGPPGKAG EGVVGPQGAR GFPGTPGLPG FKGEPGAPGE NGTPGQTGAR GLPGERGRVG APGPAGSRGS DGSVGPVGPA GPIGSAGPPG FPGAPGPKGE LGPVGNTGPG PAGPRGEQGL PGVSGPVGPP GNPGANGLTG AKGAAGLPGV AGAPGLPGPR TGARGLVGEP GPAGSKGESG GKGEPGSAGP QGPPGSSGEE GKRGPSGESG STGPTGPPGL RGGPGSRGLP GADGRAGVIG PAGARGASGP AGVRGPSGDT GRPGEPGLMG ARGLPGSPGN VGPAGKEGPA GLPGIDGRPG PIGPAGARGE AGNIGFPGPK GPAGDPGKGE KGHAGLAGNR GAPGPDGNNG AQGPPGLQGV QGG //