Q9HCB6 (SPON1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spondin-1

Alternative name(s):
F-spondin
Vascular smooth muscle cell growth-promoting factor

Gene names

Name:	SPON1
Synonyms:	KIAA0762, VSGP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	807 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	Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS By similarity. Major factor for vascular smooth muscle cell.
Subunit structure	Binds to the central extracellular domain of APP and inhibits beta-secretase cleavage of APP By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Highest expression in lung, lower expression in brain, heart, kidney, liver and testis, and lowest expression in pancreas, skeletal muscle and ovary. Not expressed in spleen. Ref.1 Ref.5
Sequence similarities	Contains 1 reelin domain. Contains 1 spondin domain. Contains 6 TSP type-1 domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APLP1	P51693	1	EBI-2431846,EBI-74648
APLP2	Q06481	1	EBI-2431846,EBI-79306
APP	P05067	1	EBI-2431846,EBI-77613

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 807

779

Spondin-1

PRO_0000035865

Regions

Domain

29 – 194

166

Reelin

Domain

195 – 388

194

Spondin

Domain

442 – 495

54

TSP type-1 1

Domain

501 – 555

55

TSP type-1 2

Domain

558 – 611

54

TSP type-1 3

Domain

614 – 666

53

TSP type-1 4

Domain

668 – 721

54

TSP type-1 5

Domain

754 – 806

53

TSP type-1 6

Amino acid modifications

Glycosylation

214

1

N-linked (GlcNAc...) Potential

Glycosylation

448

1

C-linked (Man) Ref.7

Glycosylation

451

1

C-linked (Man); partial Ref.7

Glycosylation

507

1

C-linked (Man) Ref.7

Glycosylation

510

1

C-linked (Man); partial Ref.7

Glycosylation

564

1

C-linked (Man) Ref.7

Glycosylation

620

1

C-linked (Man); partial Ref.7

Glycosylation

623

1

C-linked (Man) Ref.7

Glycosylation

674

1

C-linked (Man) Ref.7

Glycosylation

681

1

N-linked (GlcNAc...) Potential

Disulfide bond

44 ↔ 128

Ref.8 Ref.9

Disulfide bond

156 ↔ 182

Ref.8 Ref.9

Disulfide bond

502 ↔ 538

By similarity

Disulfide bond

513 ↔ 517

By similarity

Disulfide bond

548 ↔ 554

By similarity

Disulfide bond

559 ↔ 595

By similarity

Disulfide bond

570 ↔ 574

By similarity

Disulfide bond

605 ↔ 610

By similarity

Disulfide bond

615 ↔ 650

By similarity

Disulfide bond

626 ↔ 630

By similarity

Disulfide bond

660 ↔ 665

By similarity

Experimental info

Sequence conflict

500

1

S → P in BAC11217. Ref.2

Sequence conflict

545

1

T → M in BAB18461. Ref.1

Sequence conflict

570

1

C → Y in BAC11217. Ref.2

Sequence conflict

605

1

C → R in BAC11217. Ref.2

Sequence conflict

695

1

I → T in AAH19825. Ref.4

Sequence conflict

729

1

L → P in BAB18461. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

807

Helix Strand Turn

Details...

Beta strand

60 – 65

6

Beta strand

70 – 72

3

Beta strand

77 – 84

8

Beta strand

94 – 99

6

Helix

107 – 109

3

Beta strand

114 – 117

4

Turn

119 – 121

3

Beta strand

122 – 125

4

Beta strand

128 – 136

9

Beta strand

140 – 148

9

Beta strand

157 – 169

13

Beta strand

178 – 181

4

Sequences

	Sequence		Length	Mass (Da)
	Q9HCB6-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: CEA84A83F206A5A5	FASTA	807	90,973
	10 20 30 40 50 60 MRLSPAPLKL SRTPALLALA LPLAAALAFS DETLDKVPKS EGYCSRILRA QGTRREGYTE 70 80 90 100 110 120 FSLRVEGDPD FYKPGTSYRV TLSAAPPSYF RGFTLIALRE NREGDKEEDH AGTFQIIDEE 130 140 150 160 170 180 ETQFMSNCPV AVTESTPRRR TRIQVFWIAP PAGTGCVILK ASIVQKRIIY FQDEGSLTKK 190 200 210 220 230 240 LCEQDSTFDG VTDKPILDCC ACGTAKYRLT FYGNWSEKTH PKDYPRRANH WSAIIGGSHS 250 260 270 280 290 300 KNYVLWEYGG YASEGVKQVA ELGSPVKMEE EIRQQSDEVL TVIKAKAQWP AWQPLNVRAA 310 320 330 340 350 360 PSAEFSVDRT RHLMSFLTMM GPSPDWNVGL SAEDLCTKEC GWVQKVVQDL IPWDAGTDSG 370 380 390 400 410 420 VTYESPNKPT IPQEKIRPLT SLDHPQSPFY DPEGGSITQV ARVVIERIAR KGEQCNIVPD 430 440 450 460 470 480 NVDDIVADLA PEEKDEDDTP ETCIYSNWSP WSACSSSTCD KGKRMRQRML KAQLDLSVPC 490 500 510 520 530 540 PDTQDFQPCM GPGCSDEDGS TCTMSEWITW SPCSISCGMG MRSRERYVKQ FPEDGSVCTL 550 560 570 580 590 600 PTEETEKCTV NEECSPSSCL MTEWGEWDEC SATCGMGMKK RHRMIKMNPA DGSMCKAETS 610 620 630 640 650 660 QAEKCMMPEC HTIPCLLSPW SEWSDCSVTC GKGMRTRQRM LKSLAELGDC NEDLEQVEKC 670 680 690 700 710 720 MLPECPIDCE LTEWSQWSEC NKSCGKGHVI RTRMIQMEPQ FGGAPCPETV QRKKCRIRKC 730 740 750 760 770 780 LRNPSIQKLR WREARESRRS EQLKEESEGE QFPGCRMRPW TAWSECTKLC GGGIQERYMT 790 800 VKKRFKSSQF TSCKDKKEIR ACNVHPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of vascular smooth muscle cell growth promoting factor from bovine ovarian follicular fluid and its cDNA cloning from bovine and human ovary." Miyamoto K., Morishita Y., Yamazaki M., Minamino N., Kangawa K., Matsuo H., Mizutani T., Yamada K., Minegishi T. Arch. Biochem. Biophys. 390:93-100(2001) [PubMed: 11368520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Ovary.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	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].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed: 9872452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-807, TISSUE SPECIFICITY. Tissue: Brain.
[6]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[7]	"C-mannosylation and O-fucosylation of thrombospondin type 1 repeats." Gonzalez de Peredo A., Klein D., Macek B., Hess D., Peter-Katalinic J., Hofsteenge J. Mol. Cell. Proteomics 1:11-18(2002) [PubMed: 12096136] [Abstract] Cited for: GLYCOSYLATION AT TRP-448; TRP-451; TRP-507; TRP-510; TRP-564; TRP-620; TRP-623 AND TRP-674.
[8]	"Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop." Nagae M., Nishikawa K., Yasui N., Yamasaki M., Nogi T., Takagi J. Acta Crystallogr. D 64:1138-1145(2008) [PubMed: 19020352] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 40-186, DISULFIDE BONDS.
[9]	"The crystal structure of the heparin-binding reelin-N domain of f-spondin." Tan K., Duquette M., Liu J.H., Lawler J., Wang J.H. J. Mol. Biol. 381:1213-1223(2008) [PubMed: 18602404] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-194, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB051390 mRNA. Translation: BAB18461.1.
AK074803 mRNA. Translation: BAC11217.1.
AK291780 mRNA. Translation: BAF84469.1.
CH471064 Genomic DNA. Translation: EAW68488.1.
CH471064 Genomic DNA. Translation: EAW68489.1.
BC019825 mRNA. Translation: AAH19825.1.
BC136513 mRNA. Translation: AAI36514.1.
BC136563 mRNA. Translation: AAI36564.1.
AB018305 mRNA. Translation: BAA34482.2.

IPI

IPI00171473.

RefSeq

NP_006099.2.

UniGene

Hs.643864.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZOT	X-ray	2.70	A/B/C/D	29-198	[»]
2ZOU	X-ray	1.45	A/B	40-186	[»]
3COO	X-ray	2.00	A/B	29-194	[»]

ProteinModelPortal

Q9HCB6.

SMR

Q9HCB6. Positions 441-499, 562-642, 615-720.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HCB6. 5 interactions.

STRING

Q9HCB6.

Proteomic databases

PRIDE

Q9HCB6.

Genome annotation databases

Ensembl

ENST00000310358; ENSP00000309297; ENSG00000152268; Homo sapiens. [Genome view]

GeneID

10418.

KEGG

hsa:10418.

Organism-specific databases

CTD

10418.

GeneCards

GC11P013940.

H-InvDB

HIX0009464.

HGNC

HGNC:11252. SPON1.

MIM

604989. gene.

PharmGKB

PA36082.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09090.

HOGENOM

HBG444783.

HOVERGEN

HBG052920.

InParanoid

Q9HCB6.

Gene expression databases

ArrayExpress

Q9HCB6.

Bgee

Q9HCB6.

CleanEx

HS_SPON1.

Genevestigator

Q9HCB6.

GermOnline

ENSG00000152268. Homo sapiens.

Family and domain databases

InterPro

IPR002861. Reeler_dom.
IPR009465. Spondin_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]

Pfam

PF02014. Reeler. 1 hit.
PF00090. TSP_1. 6 hits.
[Graphical view]

SMART

SM00209. TSP1. 6 hits.
[Graphical view]

SUPFAM

SSF82895. TSP1. 6 hits.

PROSITE

PS51019. REELIN. 1 hit.
PS51020. SPONDIN. 1 hit.
PS50092. TSP1. 6 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

39482.

SOURCE

Search...

Entry information

Entry name

SPON1_HUMAN

Accession

Primary (citable) accession number: Q9HCB6
Secondary accession number(s): A8K6W5 , O94862, Q8NCD7, Q8WUR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	September 27, 2004
Last modified:	August 10, 2010
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.