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Database: UniProt
Entry: A0A2Y9F2W8_PHYMC
LinkDB: A0A2Y9F2W8_PHYMC
Original site: A0A2Y9F2W8_PHYMC 
ID   A0A2Y9F2W8_PHYMC        Unreviewed;      3209 AA.
AC   A0A2Y9F2W8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Collagen alpha-3(VI) chain isoform X2 {ECO:0000313|RefSeq:XP_007114153.2};
GN   Name=COL6A3 {ECO:0000313|RefSeq:XP_007114153.2};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007114153.2};
RN   [1] {ECO:0000313|RefSeq:XP_007114153.2}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007114153.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_007114153.2; XM_007114091.4.
DR   Proteomes; UP000248484; Chromosome 2.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; 3.
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; 12.
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; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00092; VWA; 12.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00327; VWA; 12.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF53300; vWA-like; 12.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50234; VWFA; 12.
PE   4: Predicted;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119,
KW   ECO:0000313|RefSeq:XP_007114153.2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..3209
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015841122"
FT   DOMAIN          38..212
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          241..414
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          444..619
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          638..815
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          836..1008
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1028..1204
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1232..1403
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1435..1608
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1638..1811
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1837..2023
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2401..2580
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2618..2814
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          3023..3121
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3144..3194
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          1612..1632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2043..2371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2888..3027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2107..2123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2131..2151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2290..2312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2922..2936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3209 AA;  347395 MW;  AC35FA822BF433FB CRC64;
     MRKHRHLPLV AIFCLFFSGF SFTHAQQQAD VKNGAAADIM FLVDSSWSIG KEHFQLVQEF
     LYDVIKSLAV GENDFRFALV WFNGSPDTEF LLNTYRSKQE VLSHVSNMSY TGGSNQTGKG
     LEYVMRNHLT EVAGSRASDG VPQVIVVLTD GHSKDALALP LAELKSADVN VFAIGVEDAD
     EGALKETASE PLNVHMFNLE NFTSLHDIVG NLVACVHSSM TPERAGGTET LKDITAQDSA
     DIIFLIDGSN NTGSVNFAVI RDFLVNLLER LSVGTQQIQV GVVQYSDEPR TLFSLNSYST
     KAQVLDAVKA LGFIGGELAN VGLALDFVLE NHFTRAGGSR VEEGVPQVLV LISAGPSSDE
     IRDAVIALKQ ASIFSFGLGA QAAPKAELQH IATNDNLVFT VPEFRSFGDV QEQLLPYIVG
     VAQRHIVLQP PTIVTQVIEI NKRDIVFLVD GSSALGLVSF NAIRDFVAKV IQRLEIGQDY
     IQVAVAQYAD TVRPEFYFNT YPTKREVVTA VRKMKPMDGS ALYTGSALDF VRNNLFTGAA
     GYRAAEGVPK LLVLITGGKS LDEVSQPAQE LKRSSIMAFA IGNKVANRAE LEEIAFDSSL
     VFIPAEFRAA PLQGVLPGLL APLRTLSGTT EVHVNKRDII FLLDGSFNVG KTNFPYVRDF
     VMNVVNSLDV GSDHIRVGLV QFSDTPVTEF SLNTYQTKAD LLAHLRQLQL KGGLGLNTGA
     ALSYVHDEHF TEAGGSRIRD RVPQLLLLFA AGQSEDSYLQ AANALARAGI LTFCVGTSQA
     NKAELEQIAF NPSLVYLMDD FSSLPALPQQ LIQPLTTYVS GGVEEVPLAQ PESKRDILFL
     FDGSANLVGQ FPAVRDFLYK VIDELDVKPD RTRVAVAQYS DDVRVESRFD EHQSKPEILN
     LVKRMKIKTG KALNLGYALD YAQRYIFVKS TGSRVEDGVL QFLVLLVAGR SSDRVDRPAL
     NLKQSGVVPF ILQAKNADPA ELEQIVPSPA FILAAESLPK IGDLQAQIVN LLKSVQNGAP
     TPVSGEKDVV FLIDGSEGVR NGFPLLKEFV QRVVESLDVG ADRVRVAVVQ YSDRTRPEFY
     LNSYMDQQSI VGAIRGLTLL GGPTPNTGAA LDFVLRNILI GSAGSRIAEG VPQLLIVLTA
     DRSGDDVRGP SVVLKRGGAV PIGVGIGNAD ITEMQTISLI PDFAVVIPTF RQLGTVQQVI
     SERVTQLSRE ELSRLRASVV PPTTPGVGGK RDVVFLIDGS QSASPEFQYI RTLIERLVDY
     LDVGFDMTRV AVIQFSEDPR VEFLLNAHSS KDEVQNAVRR LRPKGGRQIN IGGALEYVSR
     NIFKRPLGSR IEEGVPQFLV LISSGKSDDE VDEPAVELKQ FGVAPLTIAR NADQEQLVKI
     SLSPEYVFSV STFRELPSLE QKLLTPITTL TSEQVQQLLA STRYPPPAVE SDAADIVFLI
     DSSDSVRPDG IAHIRDFVSR IVRRLNIGPN KVRIGVVQFS NDVFPEFYLK TYKSQANVLD
     AIRRLRFKGG SPLNTGKALE FVARNFFVKS AGSRIEDGVP QHLVLFLGGK SQDDVSRYSQ
     VISSSGIVSL GIGDRNIDRM ELQTITNDSR LVFTVREFRE LPNIEERVMN SFGPSKVTPA
     PPGVDTPSPS RPETKKADIV FLLDGSINFR RDSFQEVLHF VSEIVDTVYE GGDSIQVGLV
     QYNSDPTDEF FLKDFSTKQQ IIDAINKVVY KGGRHANTKV GLEHLRLNHF VPEAGSRLDQ
     RVPQIAFVIT GGRSVEDAQE ASLALTQRGV KVFAVGVKNI DSEEVGKIAS NSATAFRVGN
     VQELSELSEQ VLETLHDAMH ETLCPGVPDV SKVCNLDVIL GFDGSRDQNI FVAQRSFESK
     MDTILNRISQ MQRISCSGSQ LPMVRVSVVA NTPSGPVEAF DFAEYQPELF EKFQNMRTQH
     PYVLTADTLK LYQNKFQQAS PDSVKVVIHF TDGVDGDLAD LQRASEQLRQ EGVRALIFVG
     LERVSNLEQL MQLEFGRGFM YSRPLRLNLL DLDYELAEQL DNIAEKACCG VPCKCSGQRG
     DRGPIGSIGP KGIPGEDGYR GYPGDEGGPG ERGPPGVNGT QGFQGCPGQR GIKGSRGFPG
     EKGELGEIGL DGLDGEDGDK GLPGISGEKG NPGRRGDKGP KGDKGERGDV GIRGDPGNSG
     QDSQQRGPKG ETGDIGPMGL PGTDGVSGGP GEPGKSGGVG RRGPSGAKGN KGGPGQPGSV
     GEQGTRGAQG PPGPTGPPGL IGEQGILGPR GSGGTAGAPG ERGRTGPLGR KGEPGDPGPK
     GSVGNRGPRG ETGDDGRDGV GSEGRRGKKG ERGFPGYPGP KGYPGEPGTD GALGPKGIRG
     RRGNSGPPGV AGQKGDPGYP GPSGYKGSRG DSMDQCALVQ SIKDKCPCCY GPLECPVFPT
     ELAFALDTSE GVTQDTFSRM RDVVLKIVDD LTIAESNCPR GARVAVVTYN NEVTTEIRFA
     DSKKKSVLQD KIKNLQVALT SKQQSLETAM SFVARNTFKR VRNGFLMRKV SVFFSNKPTT
     ESPQLREAVL KLSDAGITPL FLTSQEDRQL VNALQINNTA VGHALVLPAS GDLTDFLKKV
     LTCHVCLDIC NIDPSCGFGS WRPSFRDRRA AGSDVDIDIA FILDSSESTT LFQFNEMRKY
     IEYLVQQLDM SPDPKASQHF ARVAVVQHAP YESMGNASVP PVKVEFSLTD YGSKEKLLAF
     LGSRMTQLQG TRALGSAIDY TIENIFESAP NPRDLKLVVL MLTGEVKNQQ LEEAQRAILQ
     AKCKGYFFVI LGIGRKVNVK ELYSFASEPN DIFFKLMDKS TELNEEPLMR FGRLLPSFIS
     SKNAFYLSPD IRKQCDWFQG DQPAKNLVQF GYKQINVPNN VTSSPTSKPV TTAKPVTTTT
     KPVTVVNLPT SKPASMRPVA ERPVAGRPMA TKPEAVKSTA TKPEAVKSTA TKPEAVKSTA
     TKPEAAKPLA SPVATKPEAT KPEVSKTATV RSAVATRPAA AKPAPARPPA AAKPMAAKPE
     APRPQAAKLA ATRPATAKPM VKAPREVHAS EITENSAKLH WERPEPPSPY LYNLTITSAH
     DQSPVLKQNL TVTDRVIGGL LPGQTYHVTV ICYLRSQVRA IYQGSFSTKK IQPPPLQTAR
     SASSSTINLV VSAERLAGSK TDICKLPKEE GTCRDFILKW YYDSVTESCA RFWYGGCGGN
     ENRFDSQDEC EKVCPPVLIK PGVIAAIGT
//
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