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Database: UniProt
Entry: A0A2I2YTB8_GORGO
LinkDB: A0A2I2YTB8_GORGO
Original site: A0A2I2YTB8_GORGO 
ID   A0A2I2YTB8_GORGO        Unreviewed;      2548 AA.
AC   A0A2I2YTB8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Collagen type VI alpha 3 chain {ECO:0000313|Ensembl:ENSGGOP00000038220.1};
GN   Name=COL6A3 {ECO:0000313|Ensembl:ENSGGOP00000038220.1};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000038220.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000038220.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000038220.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000038220.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; CABD030019316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSGGOT00000053934.1; ENSGGOP00000038220.1; ENSGGOG00000002468.3.
DR   GeneTree; ENSGT00940000156462; -.
DR   Proteomes; UP000001519; Chromosome 2B.
DR   Bgee; ENSGGOG00000002468; Expressed in heart 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:0016020; C:membrane; 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; 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:SF13; COLLAGEN ALPHA-3(VI) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 4.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..208
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          225..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          1772..1951
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1989..2185
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2362..2456
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2483..2533
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          1000..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1429..1747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2229..2258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2328..2357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2444..2464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1496..1512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1665..1687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2548 AA;  275968 MW;  7729902CC6CC2EA7 CRC64;
     TGVCPHARLI FVFLVVMGFP LVGQAVIEVN KRDIVFLVDG SSALGLANFN AIRDFIAKVI
     QRLEIGQDLI QVAVAQYADT VRPEFYFNTH PTKREVITAV RKMKPLDGSA LYTGSALDFV
     RNNLFTSSAG YRAAEGIPKL LVLITGGKSL DEISQPAQEL KRSSIMAFAI GNKGADQAEL
     EEIAFDSSLV FIPAEFRAAP LQGMLPGLLA PLRTLSGTPE ESKRDILFLF DGSANLVGQF
     PVVRDFLYKI IDELDVKPDG TRIAVAQYSD DVKVESRFDE HQSKPEILNL VKRMKIKTGK
     ALNLGYALDY AQRYIFVKSA GSRIEDGVLQ FLVLLVAGRS SDRVDGPASN LKQSGVVPFI
     FQAKNADPAE LEQIVLSPAF ILAAESLPKI GDLQPQIVNL LKSVHNGAPA PVSGEKDVVF
     LLDGSEGVRS GFPLLKEFVQ RVVESLDVGQ DRVRVAVVQY SDRTRPEFYL NSYMNQQDVV
     NAVRQLTLLG GPTPNTGAAL EFVLRNILVS SAGSRITEGV PQLLIVLTAD RSGDDVRNPS
     VVVKRGGAVP IGIGIGNADI TEMQTISFIP DFAVAIPTFR QLGTVQQVIS ERVTQLTRKE
     LSRLQPVLQP LPSPGVGGKR DVVFLIDGSQ SAGPEFQYIR TLIERLVDYL DVGFDTTRVA
     VIQFSDDPKV EFLLNAHSSK DEVQNAVQRL RPKGGRQINV GSALEYVSRN IFKRPLGSRI
     EEGVPQFLVL ILSGKSDDEV DDPAVELKQF GVAPFTIARN ADQEELVKIS LSPEYVFSVS
     TFRELPSLEQ KLLTPITTLT SEQIQKLLAS TRYPPPAVES DAADIVFLID SSEGVRPDGF
     AHIRDFVSRI VRRLNIGPSK VRVGVVQFSN DVFPEFYLKT YRSQAPVLDA IRRLRLRGGS
     PLNTGKALEF VARNLFVKSA GSRIEDGVPQ HLVLVLGGKS QDDVSRFAQV IRSSGIVSLG
     VGDRNIDRTE LQTITNDPRL VFTVREFREL PNIEERIMNS FGPSAATPAP PGVDTPPPSR
     PEKKKADIVF LLDGSINFRR DSFQEVLRFV SEIVDTVYED GDSIQVGLVQ YNSDPTDEFF
     LKDFSTKRQI IDAINKVVYK GGRHANTKVG LEHLRVNHFV PEAGSRLDQR VPQIAFVITG
     GKSVEDAQDV SLALTQRGVK VFAVGVRNID SEEVGKIASN SATAFRVGNV QELSELSEQV
     LETLHDAMHE TLCPGVTDAA KACNLDVILG FDGSRDQNVF VAQKGFESKV DAILNRISQM
     HRVSCSGGRS PTVRVSVVAN TPSGPVEAFD FDEYQPEMLE KFRNMRSQHP YVLTEDTLKV
     YLNKFRQSSP DSVKVVIHFT DGADGDLADL HRASENLRQE GVRALILVGL ERVANLERLM
     HVEFGRGFMY DRPLRLNLLD LDYELAEQLD NIAEKACCGV PCKCSGQRGD RGPIGSIGPK
     GIPGEDGYRG YPGDEGGPGE RGPPGVNGTQ GFQGCPGQRG VKGSRGFPGE KGEVGEIGLD
     GLDGEDGDKG LPGSSGEKGN PGRRGDKGPR GEKGERGDVG IRGDPGNPGQ DSQERGPKGE
     TGDLGPMGVP GRDGVPGGPG ETGKNGGFGR RGPPGAKGNK GGPGQPGFEG EQGTRGAQGP
     AGPAGPPGLI GEQGISGPRV SLGHIAKQAE KPGPKGGIGN RGPRGETGDD GRDGVGSEGR
     RGKKGERGFP GYPGPKGNPG EPGLNGTTGP KGIRGRRGNS GPPGIVGQKG DPGYPGPAGP
     KGNRGDSIDQ CALIQSIKDK CRPLECPVFP TELAFALDTS EGVNQDTFGR MRDVVLSIVN
     DLTIAESNCP RGARVAVVTY NNEVTTEIRF ADSKRKSVLL DKIKNLQVAL TSKQQSLETA
     MSFVARNTFK RVRNGFLMRK VAVFFSNTPT RASPQLREAV LKLSDAGITP LFLTRQEDRQ
     LINALQINNT AVGHALVLPA GRDLTDFLEN VLTCHVCLDI CNIDPSCGFG SWRPSFRDRR
     AAGSDVDIDM AFILDSAETT TLFQFNEMKK YVAYLVRQLD MSPDPKASQH FARVAVVQHA
     PSESVDNASM PPVKVEFSLT DYGSKEKLVD FLSRGMTQLQ GTRALGSAIE YTIENVFESA
     PNPRDLKIVV LMLTGEVPEQ QLEEAQRVIL QAKCKGYFFV VLGIGRKVNI KEVYTFASEP
     NDVFFKLVDK STELNEEPLM RFGRLLPSFV SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK
     FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT KPVTTTTKPV TTTTKPVIIV NQASVKPPAP
     VKPAPAKPVA AKPVATKTAT VRPPVAVKPA TAAKPVAAKP AAVRPPAAAA AKPVATKPEV
     PRPQAAKPAA TKPATTKPVV KMSREVQVFE ITENSAKLHW ERPEPPGPYF YDLTVTSAHD
     QSLVLKQNLT VTDRVIGGLL AGQTYHVAVV CYLRSQVRAT YHGSFSTKKS QPPPPQPARS
     ASSSTINLMV STEPLALTET DICKLPKDEG TCRDFILKWY YDPNTKSCAR FWYGGCGGNE
     NKFGSQKECE KVCAPVLAKP GVISVMGT
//
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