Q9BU40 (CRDL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chordin-like protein 1

Alternative name(s):
Neuralin-1
Neurogenesin-1
Ventroptin

Gene names

Name:	CHRDL1
Synonyms:	NRLN1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antagonizes the function of BMP4 by binding to it and preventing its interaction with receptors. Alters the fate commitment of neural stem cells from gliogenesis to neurogenesis. Contributes to neuronal differentiation of neural stem cells in the brain by preventing the adoption of a glial fate. May play a crucial role in dorsoventral axis formation. May play a role in embryonic bone formation By similarity. May also play an important role in regulating retinal angiogenesis through modulation of BMP4 actions in endothelial cells. Plays a role during anterior segment eye development. Ref.1 Ref.6
Subcellular location	Secreted Potential.
Tissue specificity	Expressed in the developing cornea and in the eye anterior segment in addition to the retina. Differentially expressed in the fetal brain. There is high expression in cerebellum and neocortex. Expressed in retinal pericytes. Ref.1 Ref.6
Induction	By hypoxia in retinal pericytes. Ref.1
Involvement in disease	Megalocornea 1, X-linked (MGC1) [MIM:309300]: An eye disorder in which the corneal diameter is bilaterally enlarged (greater than 13 mm) without an increase in intraocular pressure. It may also be referred to as anterior megalophthalmos, since the entire anterior segment is larger than normal. Features of megalocornea in addition to a deep anterior chamber include astigmatic refractive errors, atrophy of the iris stroma, miosis secondary to decreased function of the dilator muscle, iridodonesis, and tremulousness, subluxation, or dislocation of the lens. Whereas most affected individuals exhibit normal ocular function, complications include cataract development and glaucoma following lenticular dislocation or subluxation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6
Sequence similarities	Contains 3 VWFC domains.
Sequence caution	The sequence AAH02909.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAU25841.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAF85795.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Osteogenesis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Repeat Signal
Molecular function	Developmental protein
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Traceable author statement. Source: Reactome cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW compound eye development Inferred from mutant phenotype Ref.6. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW ossification Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BU40-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BU40-2)

The sequence of this isoform differs from the canonical sequence as follows:
     95-95: D → ED
     323-323: E → EE

Isoform 3 (identifier: Q9BU40-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM
     95-173: Missing.
     323-323: E → EE

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9BU40-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM
     95-95: D → ED
     323-323: E → EE

Isoform 5 (identifier: Q9BU40-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM
     323-323: E → EE

Note: No experimental confirmation available.

Isoform 6 (identifier: Q9BU40-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRKKWKM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 450	429	Chordin-like protein 1		PRO_0000005368
Regions
	Domain	29 – 94	66	VWFC 1
	Domain	107 – 173	67	VWFC 2
	Domain	252 – 317	66	VWFC 3
	Motif	173 – 175	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1	1	M → MRKKWKM in isoform 3, isoform 4, isoform 5 and isoform 6.		VSP_043260
	Alternative sequence	95 – 173	79	Missing in isoform 3.		VSP_043261
	Alternative sequence	95	1	D → ED in isoform 2 and isoform 4.		VSP_036469
	Alternative sequence	323	1	E → EE in isoform 2, isoform 3, isoform 4 and isoform 5.		VSP_036470
	Natural variant	254	1	C → F in MGC1. Ref.6		VAR_068175

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D5F39AB9E2EE3E71	FASTA	450	51,168
	10 20 30 40 50 60 MGGMKYIFSL LFFLLLEGGK TEQVKHSETY CMFQDKKYRV GERWHPYLEP YGLVYCVNCI 70 80 90 100 110 120 CSENGNVLCS RVRCPNVHCL SPVHIPHLCC PRCPDSLPPV NNKVTSKSCE YNGTTYQHGE 130 140 150 160 170 180 LFVAEGLFQN RQPNQCTQCS CSEGNVYCGL KTCPKLTCAF PVSVPDSCCR VCRGDGELSW 190 200 210 220 230 240 EHSDGDIFRQ PANREARHSY HRSHYDPPPS RQAGGLSRFP GARSHRGALM DSQQASGTIV 250 260 270 280 290 300 QIVINNKHKH GQVCVSNGKT YSHGESWHPN LRAFGIVECV LCTCNVTKQE CKKIHCPNRY 310 320 330 340 350 360 PCKYPQKIDG KCCKVCPGKK AKELPGQSFD NKGYFCGEET MPVYESVFME DGETTRKIAL 370 380 390 400 410 420 ETERPPQVEV HVWTIRKGIL QHFHIEKISK RMFEELPHFK LVTRTTLSQW KIFTEGEAQI 430 440 450 SQMCSSRVCR TELEDLVKVL YLERSEKGHC
	Isoform 2 [UniParc]. Checksum: E214F9A68D8EE072	FASTA	452	51,426
	10 20 30 40 50 60 MGGMKYIFSL LFFLLLEGGK TEQVKHSETY CMFQDKKYRV GERWHPYLEP YGLVYCVNCI 70 80 90 100 110 120 CSENGNVLCS RVRCPNVHCL SPVHIPHLCC PRCPEDSLPP VNNKVTSKSC EYNGTTYQHG 130 140 150 160 170 180 ELFVAEGLFQ NRQPNQCTQC SCSEGNVYCG LKTCPKLTCA FPVSVPDSCC RVCRGDGELS 190 200 210 220 230 240 WEHSDGDIFR QPANREARHS YHRSHYDPPP SRQAGGLSRF PGARSHRGAL MDSQQASGTI 250 260 270 280 290 300 VQIVINNKHK HGQVCVSNGK TYSHGESWHP NLRAFGIVEC VLCTCNVTKQ ECKKIHCPNR 310 320 330 340 350 360 YPCKYPQKID GKCCKVCPGK KAKEELPGQS FDNKGYFCGE ETMPVYESVF MEDGETTRKI 370 380 390 400 410 420 ALETERPPQV EVHVWTIRKG ILQHFHIEKI SKRMFEELPH FKLVTRTTLS QWKIFTEGEA 430 440 450 QISQMCSSRV CRTELEDLVK VLYLERSEKG HC
	Isoform 3 [UniParc]. Checksum: EA581757BD2A66F2	FASTA	378	43,516
	10 20 30 40 50 60 MRKKWKMGGM KYIFSLLFFL LLEGGKTEQV KHSETYCMFQ DKKYRVGERW HPYLEPYGLV 70 80 90 100 110 120 YCVNCICSEN GNVLCSRVRC PNVHCLSPVH IPHLCCPRCP GDGELSWEHS DGDIFRQPAN 130 140 150 160 170 180 REARHSYHRS HYDPPPSRQA GGLSRFPGAR SHRGALMDSQ QASGTIVQIV INNKHKHGQV 190 200 210 220 230 240 CVSNGKTYSH GESWHPNLRA FGIVECVLCT CNVTKQECKK IHCPNRYPCK YPQKIDGKCC 250 260 270 280 290 300 KVCPGKKAKE ELPGQSFDNK GYFCGEETMP VYESVFMEDG ETTRKIALET ERPPQVEVHV 310 320 330 340 350 360 WTIRKGILQH FHIEKISKRM FEELPHFKLV TRTTLSQWKI FTEGEAQISQ MCSSRVCRTE 370 LEDLVKVLYL ERSEKGHC
	Isoform 4 [UniParc]. Checksum: 2E6FD80F2B44960F	FASTA	458	52,284
	10 20 30 40 50 60 MRKKWKMGGM KYIFSLLFFL LLEGGKTEQV KHSETYCMFQ DKKYRVGERW HPYLEPYGLV 70 80 90 100 110 120 YCVNCICSEN GNVLCSRVRC PNVHCLSPVH IPHLCCPRCP EDSLPPVNNK VTSKSCEYNG 130 140 150 160 170 180 TTYQHGELFV AEGLFQNRQP NQCTQCSCSE GNVYCGLKTC PKLTCAFPVS VPDSCCRVCR 190 200 210 220 230 240 GDGELSWEHS DGDIFRQPAN REARHSYHRS HYDPPPSRQA GGLSRFPGAR SHRGALMDSQ 250 260 270 280 290 300 QASGTIVQIV INNKHKHGQV CVSNGKTYSH GESWHPNLRA FGIVECVLCT CNVTKQECKK 310 320 330 340 350 360 IHCPNRYPCK YPQKIDGKCC KVCPGKKAKE ELPGQSFDNK GYFCGEETMP VYESVFMEDG 370 380 390 400 410 420 ETTRKIALET ERPPQVEVHV WTIRKGILQH FHIEKISKRM FEELPHFKLV TRTTLSQWKI 430 440 450 FTEGEAQISQ MCSSRVCRTE LEDLVKVLYL ERSEKGHC
	Isoform 5 [UniParc]. Checksum: E306E04B501FE8D1	FASTA	457	52,155
	10 20 30 40 50 60 MRKKWKMGGM KYIFSLLFFL LLEGGKTEQV KHSETYCMFQ DKKYRVGERW HPYLEPYGLV 70 80 90 100 110 120 YCVNCICSEN GNVLCSRVRC PNVHCLSPVH IPHLCCPRCP DSLPPVNNKV TSKSCEYNGT 130 140 150 160 170 180 TYQHGELFVA EGLFQNRQPN QCTQCSCSEG NVYCGLKTCP KLTCAFPVSV PDSCCRVCRG 190 200 210 220 230 240 DGELSWEHSD GDIFRQPANR EARHSYHRSH YDPPPSRQAG GLSRFPGARS HRGALMDSQQ 250 260 270 280 290 300 ASGTIVQIVI NNKHKHGQVC VSNGKTYSHG ESWHPNLRAF GIVECVLCTC NVTKQECKKI 310 320 330 340 350 360 HCPNRYPCKY PQKIDGKCCK VCPGKKAKEE LPGQSFDNKG YFCGEETMPV YESVFMEDGE 370 380 390 400 410 420 TTRKIALETE RPPQVEVHVW TIRKGILQHF HIEKISKRMF EELPHFKLVT RTTLSQWKIF 430 440 450 TEGEAQISQM CSSRVCRTEL EDLVKVLYLE RSEKGHC
	Isoform 6 [UniParc]. Checksum: 345A3C739493A545	FASTA	456	52,026
	10 20 30 40 50 60 MRKKWKMGGM KYIFSLLFFL LLEGGKTEQV KHSETYCMFQ DKKYRVGERW HPYLEPYGLV 70 80 90 100 110 120 YCVNCICSEN GNVLCSRVRC PNVHCLSPVH IPHLCCPRCP DSLPPVNNKV TSKSCEYNGT 130 140 150 160 170 180 TYQHGELFVA EGLFQNRQPN QCTQCSCSEG NVYCGLKTCP KLTCAFPVSV PDSCCRVCRG 190 200 210 220 230 240 DGELSWEHSD GDIFRQPANR EARHSYHRSH YDPPPSRQAG GLSRFPGARS HRGALMDSQQ 250 260 270 280 290 300 ASGTIVQIVI NNKHKHGQVC VSNGKTYSHG ESWHPNLRAF GIVECVLCTC NVTKQECKKI 310 320 330 340 350 360 HCPNRYPCKY PQKIDGKCCK VCPGKKAKEL PGQSFDNKGY FCGEETMPVY ESVFMEDGET 370 380 390 400 410 420 TRKIALETER PPQVEVHVWT IRKGILQHFH IEKISKRMFE ELPHFKLVTR TTLSQWKIFT 430 440 450 EGEAQISQMC SSRVCRTELE DLVKVLYLER SEKGHC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chordin-like 1, a bone morphogenetic protein-4 antagonist, is upregulated by hypoxia in human retinal pericytes and plays a role in regulating angiogenesis." Kane R., Godson C., O'Brien C. Mol. Vis. 14:1138-1148(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5). Tissue: Astrocyte, Brain and Uterus.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[6]	"X-linked megalocornea caused by mutations in CHRDL1 identifies an essential role for ventroptin in anterior segment development." Webb T.R., Matarin M., Gardner J.C., Kelberman D., Hassan H., Ang W., Michaelides M., Ruddle J.B., Pennell C.E., Yazar S., Khor C.C., Aung T., Yogarajah M., Robson A.G., Holder G.E., Cheetham M.E., Traboulsi E.I., Moore A.T. , Sowden J.C., Sisodiya S.M., Mackey D.A., Tuft S.J., Hardcastle A.J. Am. J. Hum. Genet. 90:247-259(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, VARIANT MGC1 PHE-254.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY608914 mRNA. Translation: AAU25841.1. Different initiation. AK293106 mRNA. Translation: BAF85795.1. Different initiation. AK297563 mRNA. Translation: BAG59955.1. AK312270 mRNA. No translation available. AL049176, AL591489 Genomic DNA. Translation: CAI42037.1. AL591489, AL049176 Genomic DNA. Translation: CAI41336.1. AL591489, AL049176 Genomic DNA. Translation: CAI41337.1. AL049176, AL591489 Genomic DNA. Translation: CAI42038.1. CH471120 Genomic DNA. Translation: EAX02656.1. CH471120 Genomic DNA. Translation: EAX02657.1. BC002909 mRNA. Translation: AAH02909.2. Different initiation.
IPI	IPI00478414. IPI00889621. IPI00921287. IPI00945674.
RefSeq	NP_001137453.1. NM_001143981.1. NP_001137454.1. NM_001143982.1. NP_001137455.2. NM_001143983.2. NP_660277.2. NM_145234.3.
UniGene	Hs.496587.
3D structure databases
ProteinModelPortal	Q9BU40.
SMR	Q9BU40. Positions 28-98, 104-174, 250-322.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BU40. 1 interaction.
STRING	9606.ENSP00000413419.
PTM databases
PhosphoSite	Q9BU40.
Polymorphism databases
DMDM	27805644.
Proteomic databases
PaxDb	Q9BU40.
PRIDE	Q9BU40.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000218054; ENSP00000218054; ENSG00000101938. ENST00000372042; ENSP00000361112; ENSG00000101938. ENST00000372045; ENSP00000361115; ENSG00000101938. ENST00000394797; ENSP00000378276; ENSG00000101938. ENST00000444321; ENSP00000399739; ENSG00000101938. ENST00000482160; ENSP00000418443; ENSG00000101938.
GeneID	91851.
KEGG	hsa:91851.
UCSC	uc004eov.3. human. uc004eow.3. human.
Organism-specific databases
CTD	91851.
GeneCards	GC0XM109917.
HGNC	HGNC:29861. CHRDL1.
HPA	HPA000226. HPA000250.
MIM	300350. gene. 309300. phenotype.
neXtProt	NX_Q9BU40.
Orphanet	91489. Isolated congenital megalocornea.
PharmGKB	PA134933380.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG147797.
HOGENOM	HOG000049211.
HOVERGEN	HBG051113.
InParanoid	Q9BU40.
OrthoDB	EOG46Q6SD.
Enzyme and pathway databases
Pathway_Interaction_DB	bmppathway. BMP receptor signaling.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q9BU40.
Bgee	Q9BU40.
CleanEx	HS_CHRDL1.
Genevestigator	Q9BU40.
GermOnline	ENSG00000101938. Homo sapiens.
Family and domain databases
InterPro	IPR001007. VWF_C. [Graphical view]
Pfam	PF00093. VWC. 3 hits. [Graphical view]
SMART	SM00214. VWC. 3 hits. [Graphical view]
PROSITE	PS01208. VWFC_1. 3 hits. PS50184. VWFC_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CHRDL1. human.
GenomeRNAi	91851.
NextBio	77488.
SOURCE	Search...

Entry information

Entry name

CRDL1_HUMAN

Accession

Primary (citable) accession number: Q9BU40
Secondary accession number(s): B1AKD0 , B4DMP3, D3DUY6, E9PGS5, Q539E4, Q9Y3H7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.