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Collagen alpha-1(XI) chain

 COBA1_HUMAN             Reviewed;        1806 AA.
P12107; B1ASK7; D3DT73; E9PCU0; Q14034; Q149N0; Q9UIT4; Q9UIT5;
Q9UIT6;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
27-SEP-2017, entry version 196.
RecName: Full=Collagen alpha-1(XI) chain;
Flags: Precursor;
Name=COL11A1; Synonyms=COLL6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANTS LEU-1323 AND
PRO-1535.
PubMed=1690726;
Yoshioka H., Ramirez F.;
"Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide
and expression of the gene in tumor cell lines.";
J. Biol. Chem. 265:6423-6426(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A; B
AND C), AND VARIANTS STL2/MARSHALL SYNDROME ARG-676; 921-GLN--PRO-926
DEL; 1313-PHE--GLY-1315 DEL; LEU-1323; VAL-1516 AND PRO-1535.
PubMed=10486316; DOI=10.1086/302585;
Annunen S., Koerkkoe J., Czarny M., Warman M.L., Brunner H.G.,
Kaeaeriaeinen H., Mulliken J.B., Tranebjaerg L., Brooks D.G.,
Cox G.F., Cruysberg J.R., Curtis M.A., Davenport S.L.H.,
Friedrich C.A., Kaitila I., Krawczynski M.R., Latos-Bielenska A.,
Mukai S., Olsen B.R., Shinno N., Somer M., Vikkula M., Zlotogora J.,
Prockop D.J., Ala-Kokko L.;
"Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall
syndrome, but other mutations cause overlapping Marshall/Stickler
phenotypes.";
Am. J. Hum. Genet. 65:974-983(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-1535.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
LEU-1323 AND PRO-1535.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 538-1806, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3182841;
Bernard M., Yoshioka H., Rodriguez E., van der Rest M., Kimura T.,
Ninomiya Y., Olsen B.R., Ramirez F.;
"Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates
that type XI belongs to the fibrillar class of collagens and reveals
that the expression of the gene is not restricted to cartilagenous
tissue.";
J. Biol. Chem. 263:17159-17166(1988).
[7]
ALTERNATIVE SPLICING.
TISSUE=Blood;
PubMed=7721876; DOI=10.1074/jbc.270.16.9486;
Zhidkova N.I., Justice S.K., Mayne R.;
"Alternative mRNA processing occurs in the variable region of the pro-
alpha 1(XI) and pro-alpha 2(XI) collagen chains.";
J. Biol. Chem. 270:9486-9493(1995).
[8]
VARIANT STL2 VAL-625.
PubMed=8872475; DOI=10.1093/hmg/5.9.1339;
Richards A.J., Yates J.R.W., Williams R., Payne S.J., Pope F.M.,
Scott J.D., Snead M.P.;
"A family with Stickler syndrome type 2 has a mutation in the COL11A1
gene resulting in the substitution of glycine 97 by valine in alpha-
1(XI) collagen.";
Hum. Mol. Genet. 5:1339-1343(1996).
[9]
VARIANTS [LARGE SCALE ANALYSIS] VAL-1326; LYS-1328 AND LEU-1328.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[10]
VARIANTS FBCG1 ARG-796 AND ARG-1042.
PubMed=21035103; DOI=10.1016/j.ajhg.2010.10.009;
Tompson S.W., Bacino C.A., Safina N.P., Bober M.B., Proud V.K.,
Funari T., Wangler M.F., Nevarez L., Ala-Kokko L., Wilcox W.R.,
Eyre D.R., Krakow D., Cohn D.H.;
"Fibrochondrogenesis results from mutations in the COL11A1 type XI
collagen gene.";
Am. J. Hum. Genet. 87:708-712(2010).
[11]
VARIANTS STL2 VAL-565; ARG-1027; 1110-VAL--PRO-1118 DEL; ASP-1513 AND
VAL-1516.
PubMed=20513134; DOI=10.1002/humu.21257;
Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S.,
Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P.;
"Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and
COL11A1.";
Hum. Mutat. 31:E1461-E1471(2010).
-!- FUNCTION: May play an important role in fibrillogenesis by
controlling lateral growth of collagen II fibrils.
-!- SUBUNIT: Trimers composed of three different chains: alpha 1(XI),
alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational
modification of alpha 1(II). Alpha 1(V) can also be found instead
of alpha 3(XI)=1(II).
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist. There is alternative
usage of exon IIA or exon IIB. Transcripts containing exon IIA
or IIB are present in cartilage, but exon IIB is preferentially
utilized in transcripts from tendon.;
Name=A;
IsoId=P12107-1; Sequence=Displayed;
Name=B;
IsoId=P12107-2; Sequence=VSP_001145;
Name=C;
IsoId=P12107-3; Sequence=VSP_001146;
Name=4;
IsoId=P12107-4; Sequence=VSP_046318;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Cartilage, placenta and some tumor or virally
transformed cell lines. Isoforms using exon IIA or IIB are found
in the cartilage while isoforms using only exon IIB are found in
the tendon.
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- DISEASE: Stickler syndrome 2 (STL2) [MIM:604841]: An autosomal
dominant form of Stickler syndrome, an inherited disorder that
associates ocular signs with more or less complete forms of Pierre
Robin sequence, bone disorders and sensorineural deafness. Ocular
disorders may include juvenile cataract, myopia, strabismus,
vitreoretinal or chorioretinal degeneration, retinal detachment,
and chronic uveitis. Pierre Robin sequence includes an opening in
the roof of the mouth (a cleft palate), a large tongue
(macroglossia), and a small lower jaw (micrognathia). Bones are
affected by slight platyspondylisis and large, often defective
epiphyses. Juvenile joint laxity is followed by early signs of
arthrosis. The degree of hearing loss varies among affected
individuals and may become more severe over time. Syndrome
expressivity is variable. {ECO:0000269|PubMed:10486316,
ECO:0000269|PubMed:20513134, ECO:0000269|PubMed:8872475}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Marshall syndrome (MRSHS) [MIM:154780]: An autosomal
dominant disorder characterized by ocular abnormalities, deafness,
craniofacial anomalies, and anhidrotic ectodermal dysplasia.
Clinical features include short stature; flat or retruded midface
with short, depressed nose, flat nasal bridge and anteverted
nares; cleft palate with or without the Pierre Robin sequence;
appearance of large eyes with ocular hypertelorism; cataracts,
either congenital or juvenile; esotropia; high myopia;
sensorineural hearing loss; spondyloepiphyseal abnormalities;
calcification of the falx cerebri; ectodermal abnormalities,
including defects in sweating and dental structures.
{ECO:0000269|PubMed:10486316}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A severe
short-limbed skeletal dysplasia characterized by broad long-bone
metaphyses, pear-shaped vertebral bodies, and characteristic
morphology of the growth plate, in which the chondrocytes have a
fibroblastic appearance and there are regions of fibrous cartilage
extracellular matrix. Clinical features include a flat midface
with a small nose and anteverted nares, significant shortening of
all limb segments but relatively normal hands and feet, and a
small bell-shaped thorax with a protuberant abdomen.
{ECO:0000269|PubMed:21035103}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
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EMBL; J04177; AAA51891.1; -; mRNA.
EMBL; AF101112; AAF04724.1; -; Genomic_DNA.
EMBL; AF101079; AAF04724.1; JOINED; Genomic_DNA.
EMBL; AF101080; AAF04724.1; JOINED; Genomic_DNA.
EMBL; AF101081; AAF04724.1; JOINED; Genomic_DNA.
EMBL; AF101082; AAF04724.1; JOINED; Genomic_DNA.
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EMBL; AL627203; CAH73908.1; -; Genomic_DNA.
EMBL; AC093150; CAH73908.1; JOINED; Genomic_DNA.
EMBL; AC099567; CAH73908.1; JOINED; Genomic_DNA.
EMBL; CH471097; EAW72908.1; -; Genomic_DNA.
EMBL; CH471097; EAW72910.1; -; Genomic_DNA.
EMBL; BC117697; AAI17698.1; -; mRNA.
EMBL; L38956; AAA79171.1; -; Genomic_DNA.
CCDS; CCDS53348.1; -. [P12107-3]
CCDS; CCDS778.1; -. [P12107-1]
CCDS; CCDS780.2; -. [P12107-4]
PIR; A35239; CGHU1E.
RefSeq; NP_001177638.1; NM_001190709.1. [P12107-3]
RefSeq; NP_001845.3; NM_001854.3. [P12107-1]
RefSeq; NP_542196.2; NM_080629.2. [P12107-2]
RefSeq; NP_542197.3; NM_080630.3. [P12107-4]
UniGene; Hs.523446; -.
ProteinModelPortal; P12107; -.
SMR; P12107; -.
BioGrid; 107698; 1.
STRING; 9606.ENSP00000359114; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P12107; -.
PhosphoSitePlus; P12107; -.
BioMuta; COL11A1; -.
DMDM; 215274245; -.
EPD; P12107; -.
MaxQB; P12107; -.
PaxDb; P12107; -.
PeptideAtlas; P12107; -.
PRIDE; P12107; -.
Ensembl; ENST00000353414; ENSP00000302551; ENSG00000060718. [P12107-3]
Ensembl; ENST00000358392; ENSP00000351163; ENSG00000060718. [P12107-2]
Ensembl; ENST00000370096; ENSP00000359114; ENSG00000060718. [P12107-1]
Ensembl; ENST00000512756; ENSP00000426533; ENSG00000060718. [P12107-4]
GeneID; 1301; -.
KEGG; hsa:1301; -.
UCSC; uc001dul.4; human. [P12107-1]
CTD; 1301; -.
DisGeNET; 1301; -.
EuPathDB; HostDB:ENSG00000060718.19; -.
GeneCards; COL11A1; -.
GeneReviews; COL11A1; -.
H-InvDB; HIX0028847; -.
HGNC; HGNC:2186; COL11A1.
HPA; HPA058335; -.
MalaCards; COL11A1; -.
MIM; 120280; gene.
MIM; 154780; phenotype.
MIM; 228520; phenotype.
MIM; 604841; phenotype.
neXtProt; NX_P12107; -.
OpenTargets; ENSG00000060718; -.
Orphanet; 250984; Autosomal recessive Stickler syndrome.
Orphanet; 2021; Fibrochondrogenesis.
Orphanet; 560; Marshall syndrome.
Orphanet; 90654; Stickler syndrome type 2.
PharmGKB; PA26702; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG41112UQ; LUCA.
GeneTree; ENSGT00840000129673; -.
HOGENOM; HOG000085654; -.
HOVERGEN; HBG004933; -.
InParanoid; P12107; -.
KO; K19721; -.
OMA; HPGKEGQ; -.
OrthoDB; EOG091G01AE; -.
PhylomeDB; P12107; -.
TreeFam; TF323987; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P12107; -.
ChiTaRS; COL11A1; human.
GeneWiki; Collagen,_type_XI,_alpha_1; -.
GenomeRNAi; 1301; -.
PMAP-CutDB; B1ASK7; -.
PRO; PR:P12107; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000060718; -.
CleanEx; HS_COL11A1; -.
ExpressionAtlas; P12107; baseline and differential.
Genevisible; P12107; HS.
GO; GO:0005592; C:collagen type XI trimer; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0050840; F:extracellular matrix binding; NAS:UniProtKB.
GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; NAS:UniProtKB.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:Ensembl.
GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0035989; P:tendon development; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR001791; Laminin_G.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 7.
Pfam; PF02210; Laminin_G_2; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00282; LamG; 1.
SMART; SM00210; TSPN; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51461; NC1_FIB; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cataract; Collagen; Complete proteome;
Deafness; Direct protein sequencing; Disease mutation; Disulfide bond;
Dwarfism; Ectodermal dysplasia; Extracellular matrix; Glycoprotein;
Hydroxylation; Metal-binding; Polymorphism; Reference proteome;
Repeat; Secreted; Signal; Stickler syndrome.
SIGNAL 1 35 {ECO:0000255}.
PROPEP 36 511 N-terminal propeptide. {ECO:0000255}.
/FTId=PRO_0000005774.
CHAIN 512 1563 Collagen alpha-1(XI) chain.
/FTId=PRO_0000005775.
PROPEP 1564 1806 C-terminal propeptide.
/FTId=PRO_0000005776.
DOMAIN 71 243 Laminin G-like.
DOMAIN 442 490 Collagen-like 1.
DOMAIN 532 586 Collagen-like 2.
DOMAIN 583 641 Collagen-like 3.
DOMAIN 616 674 Collagen-like 4.
DOMAIN 643 699 Collagen-like 5.
DOMAIN 1393 1450 Collagen-like 6.
DOMAIN 1429 1487 Collagen-like 7.
DOMAIN 1483 1541 Collagen-like 8.
DOMAIN 1577 1805 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 230 419 Nonhelical region.
REGION 420 508 Triple-helical region (interrupted).
REGION 509 511 Short nonhelical segment.
REGION 512 528 Telopeptide.
REGION 529 1542 Triple-helical region.
REGION 1543 1563 Nonhelical region (C-terminal).
METAL 1625 1625 Calcium. {ECO:0000250}.
METAL 1627 1627 Calcium. {ECO:0000250}.
METAL 1628 1628 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1630 1630 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1633 1633 Calcium. {ECO:0000250}.
MOD_RES 612 612 Allysine.
MOD_RES 1452 1452 Allysine.
CARBOHYD 1640 1640 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 61 243 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 182 236 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1607 1639 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1630 1630 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793}.
DISULFID 1648 1803 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1714 1757 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VAR_SEQ 261 299 YAPEDIIEYDYEYGEAEYKEAESVTEGPTVTEETIAQTE
-> KKKSNFKKKMRTVATKSKEKSKKFTPPKSEKFSSKKKK
SYQASAKAKLGVK (in isoform B).
{ECO:0000305}.
/FTId=VSP_001145.
VAR_SEQ 261 299 Missing (in isoform C). {ECO:0000305}.
/FTId=VSP_001146.
VAR_SEQ 300 415 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046318.
VARIANT 8 8 W -> G (in dbSNP:rs12025888).
/FTId=VAR_047723.
VARIANT 46 46 D -> E (in dbSNP:rs11164663).
/FTId=VAR_047724.
VARIANT 559 559 G -> S (in dbSNP:rs12143815).
/FTId=VAR_047725.
VARIANT 565 565 G -> V (in STL2).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063675.
VARIANT 625 625 G -> V (in STL2; dbSNP:rs121912943).
{ECO:0000269|PubMed:8872475}.
/FTId=VAR_013583.
VARIANT 676 676 G -> R (in STL2; overlapping phenotype
with Marshall syndrome;
dbSNP:rs749663226).
{ECO:0000269|PubMed:10486316}.
/FTId=VAR_013584.
VARIANT 796 796 G -> R (in FBCG1).
{ECO:0000269|PubMed:21035103}.
/FTId=VAR_065904.
VARIANT 921 926 Missing (in STL2; overlapping phenotype
with Marshall syndrome).
{ECO:0000269|PubMed:10486316}.
/FTId=VAR_013585.
VARIANT 1027 1027 G -> R (in STL2).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063676.
VARIANT 1042 1042 G -> R (in FBCG1).
{ECO:0000269|PubMed:21035103}.
/FTId=VAR_065905.
VARIANT 1110 1118 Missing (in STL2).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063677.
VARIANT 1313 1315 Missing (in STL2; overlapping phenotype
with Marshall syndrome).
{ECO:0000269|PubMed:10486316}.
/FTId=VAR_013586.
VARIANT 1323 1323 P -> L (in dbSNP:rs3753841).
{ECO:0000269|PubMed:10486316,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1690726}.
/FTId=VAR_047726.
VARIANT 1326 1326 A -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035743.
VARIANT 1328 1328 Q -> K (in a breast cancer sample;
somatic mutation; dbSNP:rs750014974).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035744.
VARIANT 1328 1328 Q -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035745.
VARIANT 1513 1513 G -> D (in STL2).
{ECO:0000269|PubMed:20513134}.
/FTId=VAR_063678.
VARIANT 1516 1516 G -> V (in STL2; overlapping phenotype
with Marshall syndrome).
{ECO:0000269|PubMed:10486316,
ECO:0000269|PubMed:20513134}.
/FTId=VAR_013587.
VARIANT 1535 1535 S -> P (in dbSNP:rs1676486).
{ECO:0000269|PubMed:10486316,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1690726,
ECO:0000269|Ref.4}.
/FTId=VAR_047727.
VARIANT 1805 1805 L -> F (in dbSNP:rs1975916).
/FTId=VAR_047728.
CONFLICT 941 944 KDGL -> RMGC (in Ref. 1; AAA51891).
{ECO:0000305}.
CONFLICT 986 986 H -> Y (in Ref. 1; AAA51891).
{ECO:0000305}.
CONFLICT 1074 1074 P -> R (in Ref. 1; AAA51891).
{ECO:0000305}.
CONFLICT 1142 1142 D -> G (in Ref. 1; AAA51891).
{ECO:0000305}.
CONFLICT 1218 1218 M -> W (in Ref. 1; AAA51891).
{ECO:0000305}.
CONFLICT 1758 1758 A -> T (in Ref. 1; AAA51891).
{ECO:0000305}.
CONFLICT 1786 1786 N -> S (in Ref. 1; AAA51891).
{ECO:0000305}.
SEQUENCE 1806 AA; 181065 MW; 7CBF744263321B43 CRC64;
MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF
CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN
EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV
DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS
PDCDSSAPKA AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEA
NIVDDFQEYN YGTMESYQTE APRHVSGTNE PNPVEEIFTE EYLTGEDYDS QRKNSEDTLY
ENKEIDGRDS DLLVDGDLGE YDFYEYKEYE DKPTSPPNEE FGPGVPAETD ITETSINGHG
AYGEKGQKGE PAVVEPGMLV EGPPGPAGPA GIMGPPGLQG PTGPPGDPGD RGPPGRPGLP
GADGLPGPPG TMLMLPFRYG GDGSKGPTIS AQEAQAQAIL QQARIALRGP PGPMGLTGRP
GPVGGPGSSG AKGESGDPGP QGPRGVQGPP GPTGKPGKRG RPGADGGRGM PGEPGAKGDR
GFDGLPGLPG DKGHRGERGP QGPPGPPGDD GMRGEDGEIG PRGLPGEAGP RGLLGPRGTP
GAPGQPGMAG VDGPPGPKGN MGPQGEPGPP GQQGNPGPQG LPGPQGPIGP PGEKGPQGKP
GLAGLPGADG PPGHPGKEGQ SGEKGALGPP GPQGPIGYPG PRGVKGADGV RGLKGSKGEK
GEDGFPGFKG DMGLKGDRGE VGQIGPRGED GPEGPKGRAG PTGDPGPSGQ AGEKGKLGVP
GLPGYPGRQG PKGSTGFPGF PGANGEKGAR GVAGKPGPRG QRGPTGPRGS RGARGPTGKP
GPKGTSGGDG PPGPPGERGP QGPQGPVGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT
GPPGPGGVVG PQGPTGETGP IGERGHPGPP GPPGEQGLPG AAGKEGAKGD PGPQGISGKD
GPAGLRGFPG ERGLPGAQGA PGLKGGEGPQ GPPGPVGSPG ERGSAGTAGP IGLPGRPGPQ
GPPGPAGEKG APGEKGPQGP AGRDGVQGPV GLPGPAGPAG SPGEDGDKGE IGEPGQKGSK
GDKGENGPPG PPGLQGPVGA PGIAGGDGEP GPRGQQGMFG QKGDEGARGF PGPPGPIGLQ
GLPGPPGEKG ENGDVGPMGP PGPPGPRGPQ GPNGADGPQG PPGSVGSVGG VGEKGEPGEA
GNPGPPGEAG VGGPKGERGE KGEAGPPGAA GPPGAKGPPG DDGPKGNPGP VGFPGDPGPP
GEPGPAGQDG VGGDKGEDGD PGQPGPPGPS GEAGPPGPPG KRGPPGAAGA EGRQGEKGAK
GEAGAEGPPG KTGPVGPQGP AGKPGPEGLR GIPGPVGEQG LPGAAGQDGP PGPMGPPGLP
GLKGDPGSKG EKGHPGLIGL IGPPGEQGEK GDRGLPGTQG SPGAKGDGGI PGPAGPLGPP
GPPGLPGPQG PKGNKGSTGP AGQKGDSGLP GPPGSPGPPG EVIQPLPILS SKKTRRHTEG
MQADADDNIL DYSDGMEEIF GSLNSLKQDI EHMKFPMGTQ TNPARTCKDL QLSHPDFPDG
EYWIDPNQGC SGDSFKVYCN FTSGGETCIY PDKKSEGVRI SSWPKEKPGS WFSEFKRGKL
LSYLDVEGNS INMVQMTFLK LLTASARQNF TYHCHQSAAW YDVSSGSYDK ALRFLGSNDE
EMSYDNNPFI KTLYDGCASR KGYEKTVIEI NTPKIDQVPI VDVMINDFGD QNQKFGFEVG
PVCFLG


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