ID A0A2R8MHM0_CALJA Unreviewed; 2513 AA.
AC A0A2R8MHM0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Collagen type VI alpha 3 chain {ECO:0000313|Ensembl:ENSCJAP00000059825.2};
GN Name=COL6A3 {ECO:0000313|Ensembl:ENSCJAP00000059825.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000059825.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000059825.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000059825.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSCJAT00000072390.3; ENSCJAP00000059825.2; ENSCJAG00000002226.6.
DR GeneTree; ENSGT00940000156462; -.
DR Proteomes; UP000008225; Chromosome 6.
DR Bgee; ENSCJAG00000002226; Expressed in ovary and 5 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd22629; Kunitz_collagen_alpha3_VI; 1.
DR CDD; cd01481; vWA_collagen_alpha3-VI-like; 2.
DR CDD; cd01450; vWFA_subfamily_ECM; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 9.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR041900; vWA_collagen_alpha3-VI-like.
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; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 9.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 9.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53300; vWA-like; 9.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50234; VWFA; 9.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 31..206
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 223..397
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 417..593
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 621..792
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 824..997
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1027..1200
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1226..1412
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1741..1920
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1958..2154
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 2327..2421
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2448..2498
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 1433..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2198..2221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2284..2323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2410..2429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2513 AA; 273156 MW; F5E7B5BAC2B8438A CRC64;
MSGHRIMHVV TCHSNCLIML PPTVIEVNKR DIVFLVDGSS ALGLANFNAI RDFIAKVIQR
LEIGQDLIQV AVAQYADTVR PEFYFNTYPA KKDIITAVRK MKPLDGSALY TGSALDFVRN
NLFTSSAGYR DADGIPKLLV LITGGKSLDE ISQPAQELKR SSIMAFAIGN KGADQAELEE
IAFDSSLVFI PAEFRAAPLQ GMLPGLLAPL RTLSGTPEES KRDILFLFDG SANLVGQGQF
PVVRDFLYKI IDELNVQPDG TRIAVAQYSD DVKVESRFDE HQSKPDILNL VKRMKIKTGK
ALNLGYALDY AQRYIFVKSA GSRIEDGVPQ FLVLLVAGRS SDRVDGPASN MKQSGIVSFI
FQAKNADPAE LEQIVLSPAF ILAAESLPKI GDLQPQIVNL LKTVHNGAPV RVSGEKDVVF
LLDGSEGVRS GFPLLKEFVQ RVVESLDVGQ DRVRVAVVQY SDRTRPEFYL NSYMNQQDIV
NAIRQLTLLG GPTPNTGAAL EFVLRNILVS SAGSRITEGV PQLLIVVTAD RSGDDVRNPS
VVLKKGGAVP IGIGIGNADI TEMQTISFIP DFAVAIPTFR QLGTIQQVIS ERVTQLTREE
LSRLQPVLQP VPSPGVGDKR DVVFLIDGSQ SAGPEFQHIR TLIERLVEFL DVGFDTTRVA
VIQFSDDPKV EFLLNAHSSK DEVQNAVRRL RPKGGRQINL GSALEYVSRN IFKRPLGSRI
EEGVPQFLVL ISSGKSDDEV DDPVVELKQF GVAPLIVARN VDEEELVKIS LSPEYVFLVS
SFQELPSLEQ KLLTPIMSLN SGHIQQLLAS THYPPPAVES DAADIVFLID SSEGVRSEGF
AHIRDFVIRI VRRLNIGPSK VRVGVVQFSN DVFPEFYLKT YRSQVPVLEA IRRLRLRGGS
PLNTGRALEF VARNFFVKSA GSRIEDGVPQ HLVLVLGGKS QDDVSRFAQV IRSSGIVSLG
VGDRNIDRTE LQTITNDPRL VFTVRDFRDL PNIEERIMNS FGPSAATPAP PGVDIPSPSL
PEKKKADIVF LLDGSINFRR DSFQEVLRFV SEIVDTVYED GDSIQVGLVQ YNSDPTDEFF
LRDFSTKRQI IDAINKVVYK GGRHANTKVG LEHLRVNHFV PEAGSRLEQR VPQIAFVVTG
GKSVEDAQQV SLALTQSGVK VFAVGVRNID SEEVGKTASN SATAFRVGNV QELSELSEQV
LETLHDAMHE TLCPGVTDVA RACNLDVILG FDGSRDQNVF VAQKGFESKV DAILNRISQM
HRVSCSGGRS PTVRVSVVGN TPSGPVEAFD FDEYQPEMLE KFRNMRSQHP YVLTADTLKV
YQNKFRQSSP DSVKVVIHFT DGADGDLADL HRASEDLRQE GVRALILVGL ERVANLERLM
HLEFGRGFMY DRPLRLNLLD LDYELAEQLD NIAEKACCGV PCKCSGQRGD RGPIGSIGPK
GIPGEDGYRG YPGDEGGPGE RGPPGVNGTQ GFQGCPGQRG IKGEVGEIGL DGLDGEEVSD
FTLNKGLPGS SGEKGNPGRR GDKGPRGVKG ERGDVGIRGD PGNPGQDSQQ RGPKGETGDI
GPMGVPGRDG VPGRPGETGK NVSAFGPLGG GNKGGPGQPG FEGEQGTRGA QVSASFKPLE
KWIKANHLAA LENVARTFPG DPAPRTLSGI FCSKAHCATS WLSSQGNPGQ PGLNGAPGPK
GIRGRRGNSG PPGIVGQKGD PGYPGPAGPK GNRGDSIDQC ALIQSIKDKC RPLECPVFPT
ELAFALDTSE GVTQDTFSRM RDVVLGIVND LTVAESNCPR GARVAVVTYN NEVTTEIRFA
DSKKKSVLLD KIKNLQVSLT SKQQSLETAM SFVARNTFKR VRNGFLMRKV AVFFSNRPTR
ASPQLGEAVL KLSDAGITPL FLTSQEDRQL INALQINNTA VGHALVLPAR RDLTDFLKNV
LTCHVCLDIC NIDPSCGFGS WRPSFRDRRA AGSDVDIDMA FILDSAETTS LFQFNEMKKY
IAYLIRQLDI SPDPKASQHF ARVAIVQHAP YESTDDASVP PVKVEFSLTD YGSKEKLLDF
LSRGMTQLQG TRALGSAIEY TIENVFKSAP NPRDLKIVVL MLTGEVQEQQ LEEAQKVILQ
AKCQGYFFVV LGIGRKVNIK EVYTFASEPN DVFFKLVDKP TELSEEPLMR FGRLLPSFVS
SENAFYLSPD IRKQCDWFQG DQPKQTLVKF GHKQVNIPNN VTSSPTSKPV TTTKPVTTAK
PVTTSTKPVT IVNQTSVKPA DAKPAPAKPA PAKPAAAKPV ATKAATVRPS VVVKPAVAAK
PAAAKPAAAR PPAAVAKPVA TKPEASRPQA AKSAATKPAT TKPVVKVSQE VQVFDITENS
AKLHWERPDP HSPYFYDLTV TSAHDQSLVL KQNLSITDRI IGGLLPGQTY HVAVVCYLKS
QVRATYHGSF STVKSQPSPP QPARSASSST INLMVSTEPL ALTETDICKL PKDEGTCRDF
ILKWYYDPNT KSCARFWYGG CGGNENKFGS QKECEKVCAP VLAKPGVVSV IGT
//
