COKA1_MOUSE
ID COKA1_MOUSE Reviewed; 1320 AA.
AC Q923P0; A8WIS2; Q91WC4; Q923P1; Q923P2; Q9D9L7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Collagen alpha-1(XX) chain;
DE Flags: Precursor;
GN Name=Col20a1;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-1320 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1131-1320 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1159-1320 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Probable collagen protein.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q923P0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q923P0-2; Sequence=VSP_038879;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24730.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL450341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016112; AAH16112.1; ALT_INIT; mRNA.
DR EMBL; BC030415; AAH30415.1; -; mRNA.
DR EMBL; AK006759; BAB24730.1; ALT_INIT; mRNA.
DR CCDS; CCDS50844.1; -. [Q923P0-1]
DR RefSeq; NP_082794.1; NM_028518.1. [Q923P0-1]
DR AlphaFoldDB; Q923P0; -.
DR SMR; Q923P0; -.
DR ComplexPortal; CPX-3003; Collagen type XX trimer.
DR STRING; 10090.ENSMUSP00000104484; -.
DR GlyGen; Q923P0; 4 sites.
DR iPTMnet; Q923P0; -.
DR PhosphoSitePlus; Q923P0; -.
DR PaxDb; Q923P0; -.
DR PRIDE; Q923P0; -.
DR ProteomicsDB; 283786; -. [Q923P0-1]
DR ProteomicsDB; 283787; -. [Q923P0-2]
DR Antibodypedia; 29690; 207 antibodies from 27 providers.
DR DNASU; 73368; -.
DR Ensembl; ENSMUST00000228434; ENSMUSP00000153871; ENSMUSG00000016356. [Q923P0-1]
DR GeneID; 73368; -.
DR KEGG; mmu:73368; -.
DR UCSC; uc008okp.2; mouse. [Q923P0-1]
DR CTD; 57642; -.
DR MGI; MGI:1920618; Col20a1.
DR VEuPathDB; HostDB:ENSMUSG00000016356; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000163709; -.
DR HOGENOM; CLU_002527_0_0_1; -.
DR InParanoid; Q923P0; -.
DR OMA; VKPVQQY; -.
DR OrthoDB; 67372at2759; -.
DR PhylomeDB; Q923P0; -.
DR TreeFam; TF329914; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 73368; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Col20a1; mouse.
DR PRO; PR:Q923P0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q923P0; protein.
DR Bgee; ENSMUSG00000016356; Expressed in seminiferous tubule of testis and 140 other tissues.
DR ExpressionAtlas; Q923P0; baseline and differential.
DR Genevisible; Q923P0; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 6.
DR Gene3D; 3.40.50.410; -; 1.
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; IPR001791; Laminin_G.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49265; SSF49265; 4.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Collagen; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1320
FT /note="Collagen alpha-1(XX) chain"
FT /id="PRO_0000393005"
FT DOMAIN 27..118
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 177..352
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 377..466
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 467..556
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 557..644
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 646..735
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 740..831
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 840..1035
FT /note="Laminin G-like"
FT DOMAIN 1069..1122
FT /note="Collagen-like 1"
FT DOMAIN 1125..1174
FT /note="Collagen-like 2"
FT DOMAIN 1165..1221
FT /note="Collagen-like 3"
FT REGION 728..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1242..1297
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038879"
FT CONFLICT 556..558
FT /note="GPP -> PRV (in Ref. 2; AAH30415)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="S -> V (in Ref. 2; AAH30415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="T -> S (in Ref. 2; AAH16112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1320 AA; 140926 MW; 4E5B1D76D8DF2978 CRC64;
MSLQGSYQHF CLWMFLGTTL ALGQGQVSSR LRLAVLPEDQ LQMKWREAEG SGLGFLVQVT
PMAGDLEQEL ILTTKTPKAT VGGLNPSKSY TLQIFELTDS GPILLARREF VIEDLKSQSL
GRGSRRLAGA TLEPTSLPLR GPDSEKTSEP SIAFTLSRDL PILDHPQFQC TPPTPADIIF
LVDGSWSIGH NHFQQVKDFL ASIITQFAIG PDKVQVGLTQ YSGDPQTEWD LNSFQTKEQV
LAAVHHLRYK GGNTFTGLAL THVLEQNLKP AAGVRPEAAK VLILVTDGKS QDDVRTAARI
LKDQDIDVFV VGVKNVDEAE LKLLASQPLD ITVHNVLDFP QLDTLAPLLS RLICQKIQGR
GPVKPAAGTR VLDPLPTPTR LILTHATSSS IHLSWTPALY PPLKYLIVWQ PSRGGAPKEV
VVEGPVSSME LGNLTSSTEY LVSVLPVYES GVGKSLQGRA TTAPLPPPGP LTLAAVTPRT
LHVTWPPSAG VTQYLVQYLL ATSTGEEQKR EVHVGQPEVL LDGLEPGQDY DVSVQSLRGP
EASEVQSIRA RTSALGPPRH LTFSDVRYNS TCVSWEAQRP VRLVKVSYIS SDGSHSGQTQ
VPGNLTSATL GPLSSSTMYT VRVTCFYLGG GSSVLTGHVT TQKAPSPGQL SVMELPGDAV
KLSWLATALS GVLVYQIKWM PLGEGKAREI SVPGTLGTAT LPGLMKHVEY EITILAYYRD
GTRSDPVSLR YTPSAASRSP PSSLALSSET PNSLQVNWTP PSGHVLHYRL NYTLASGSGP
EKSISVPGTR SHAVLRDLMS ATKYRVLVSA VYRAGESMAV SATYRTAACP ALHPDSSLSG
FDLMVAFGLV AKEYASIRGV AMEPSALGVV PTFTLFKDAQ LMRRVSDIYP ATLPPEHTIV
FLVRLLPETP REAFALWQMM AEDFQPILGV LLDAGRKSLT YFNHDSRAAL QEVTFDLQDA
KKIFFGSFHK VHIAVGHSKV RLYVDCRKVA ERPIGDAGSP PTGGFITLGR LAKARGPRSS
SATFQLQMLQ IVCSDTWADK DRCCEIPALR DGETCPAFPS ACAYSSETPG PPGPQGPPGL
PGRNGPPGQQ GHPGPKGEPG PPGQTGPEGP GGQQGSPGTQ GRAVQGPMGP PGAKGEKGDQ
GLSGLQGLSG QQGIPGKTGL QGPKGMRGLE GPAGLPGPPG PRGFQGLAGA RGTNGERGAP
GAVGPTGLPG SKGERGEKGE PQSLATIFQL VSQACESAIR THVLKLNSFL HENARPPMPF
MAETAKLGRP RSIDPGLHNE ALLPGDWGHI LRPEDQGEPV TISHTSNPRL QEVQTPESLE
