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Database: UniProt
Entry: A0A2I2Y9U4_GORGO
LinkDB: A0A2I2Y9U4_GORGO
Original site: A0A2I2Y9U4_GORGO 
ID   A0A2I2Y9U4_GORGO        Unreviewed;      2537 AA.
AC   A0A2I2Y9U4;
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:ENSGGOP00000031681.1};
GN   Name=COL6A3 {ECO:0000313|Ensembl:ENSGGOP00000031681.1};
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:ENSGGOP00000031681.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000031681.1, 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:ENSGGOP00000031681.1, 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:ENSGGOP00000031681.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; CABD030019316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSGGOT00000064778.1; ENSGGOP00000031681.1; 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; 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   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          1761..1940
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1978..2174
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2351..2445
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2472..2522
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..1734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2218..2247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2317..2346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2433..2453
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        1663..1683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2537 AA;  274634 MW;  C939CF744888EFEE 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 ETGKNVSAIR ALGGSGNKGG PGQPGFEGEQ GTRGAQGPAG
     PAGPPGLIGE QGISGPRVSL GHIAKQAEKP GPKGGIGNRG PRGETGDDGR DGVGSEGRRG
     KKGNPGEPGL NGTTGPKGIR GRRGNSGPPG IVGQKGDPGY PGPAGPKGNR GDSIDVSSIL
     SLTLRPPLST GPLECPVFPT ELAFALDTSE GVNQDTFGRM RDVVLSIVND LTIAESNCPR
     GARVAVVTYN NEVTTEIRFA DSKRKSVLLD KIKNLQVALT SKQQSLETAM SFVARNTFKR
     VRNGFLMRKV AVFFSNTPTR ASPQLREAVL KLSDAGITPL FLTRQEDRQL INALQINNTA
     VGHALVLPAG RDLTDFLENV LTCHVCLDIC NIDPSCGFGS WRPSFRDRRA AGSDVDIDMA
     FILDSAETTT LFQFNEMKKY VAYLVRQLDM SPDPKASQHF ARVAVVQHAP SESVDNASMP
     PVKVEFSLTD YGSKEKLVDF LSRGMTQLQG TRALGSAIEY TIENVFESAP NPRDLKIVVL
     MLTGEVPEQQ LEEAQRVILQ AKCKGYFFVV LGIGRKVNIK EVYTFASEPN DVFFKLVDKS
     TELNEEPLMR FGRLLPSFVS SENAFYLSPD IRKQCDWFQG DQPTKNLVKF GHKQVNVPNN
     VTSSPTSNPV TTTKPVTTTK PVTTTTKPVT TTTKPVIIVN QASVKPPAPV KPAPAKPVAA
     KPVATKTATV RPPVAVKPAT AAKPVAAKPA AVRPPAAAAA KPVATKPEVP RPQAAKPAAT
     KPATTKPVVK MSREVQVFEI TENSAKLHWE RPEPPGPYFY DLTVTSAHDQ SLVLKQNLTV
     TDRVIGGLLA GQTYHVAVVC YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS
     TEPLALTETD ICKLPKDEGT CRDFILKWYY DPNTKSCARF WYGGCGGNEN KFGSQKECEK
     VCAPVLAKPG VISVMGT
//
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